MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins. A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins. FEBS letters 2016 imex curation Louros NN., Chrysina ED., Baltatzis GE., Patsouris ES., Hamodrakas SJ., Iconomidou VA. veconom@biol.uoa.gr 8-Jun-2017: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Louros NN., Chrysina ED., Baltatzis GE., Patsouris ES., Hamodrakas SJ., Iconomidou VA. veconom@biol.uoa.gr Accepted 2017-MAY-08 AT 10:26 BST AT 10:26 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins. A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins. FEBS letters 2016 imex curation Louros NN., Chrysina ED., Baltatzis GE., Patsouris ES., Hamodrakas SJ., Iconomidou VA. veconom@biol.uoa.gr 8-Jun-2017: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Louros NN., Chrysina ED., Baltatzis GE., Patsouris ES., Hamodrakas SJ., Iconomidou VA. veconom@biol.uoa.gr Accepted 2017-MAY-08 AT 10:26 BST AT 10:26 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins. A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins. FEBS letters 2016 imex curation Louros NN., Chrysina ED., Baltatzis GE., Patsouris ES., Hamodrakas SJ., Iconomidou VA. veconom@biol.uoa.gr 8-Jun-2017: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro ir spectrometry infrared spectroscopy ir spectrometry predetermined predetermined participant predetermined Louros NN., Chrysina ED., Baltatzis GE., Patsouris ES., Hamodrakas SJ., Iconomidou VA. veconom@biol.uoa.gr Accepted 2017-MAY-08 AT 10:26 BST AT 10:26 BST by MARTA FEBS letters 2016 Only protein-protein interactions imex curation imex curation zp3_human Zona pellucida sperm-binding protein 3 ZP3 ZP3A ZP3B ZPC Sperm receptor ZP3A/ZP3B Zona pellucida glycoprotein 3 Zona pellucida protein C protein protein human Homo sapiens Human MELSYRLFICLLLWGSTELCYPQPLWLLQGGASHPETSVQPVLVECQEATLMVMVSKDLFGTGKLIRAADLTLGPEACEPLVSMDTEDVVRFEVGLHECGNSMQVTDDALVYSTFLLHDPRPVGNLSIVRTNRAEIPIECRYPRQGNVSSQAILPTWLPFRTTVFSEEKLTFSLRLMEENWNAEKRSPTFHLGDAAHLQAEIHTGSHVPLRLFVDHCVATPTPDQNASPYHTIVDFHGCLVDGLTDASSAFKVPRPGPDTLQFTVDVFHFANDSRNMIYITCHLKVTLAEQDPDELNKACSFSKPSNSWFPVEGSADICQCCNKGDCGTPSHSRRQPHVMSQWSRSASRNRRHVTEEADVTVGPLIFLDRRGDHEVEQWALPSDTSVVLLGVGLAVVVSLTLTAVILVLTRRCRTASHPVSASE 0F3CCDA2427C0E3A zp4_human Zona pellucida sperm-binding protein 4 ZP4 ZPB Zona pellucida glycoprotein 4 Zona pellucida protein B protein protein human Homo sapiens Human MWLLRCVLLCVSLSLAVSGQHKPEAPDYSSVLHCGPWSFQFAVNLNQEATSPPVLIAWDNQGLLHELQNDSDCGTWIRKGPGSSVVLEATYSSCYVTEWDSHYIMPVGVEGAGAAEHKVVTERKLLKCPMDLLARDAPDTDWCDSIPARDRLPCAPSPISRGDCEGLGCCYSSEEVNSCYYGNTVTLHCTREGHFSIAVSRNVTSPPLLLDSVRLALRNDSACNPVMATQAFVLFQFPFTSCGTTRQITGDRAVYENELVATRDVKNGSRGSVTRDSIFRLHVSCSYSVSSNSLPINVQVFTLPPPFPETQPGPLTLELQIAKDKNYGSYYGVGDYPVVKLLRDPIYVEVSILHRTDPYLGLLLQQCWATPSTDPLSQPQWPILVKGCPYIGDNYQTQLIPVQKALDLPFPSHHQRFSIFTFSFVNPTVEKQALRGPVHLHCSVSVCQPAETPSCVVTCPDLSRRRNFDNSSQNTTASVSSKGPMILLQATKDPPEKLRVPVDSKVLWVAGLSGTLILGALLVSYLAVKKQKSCPDQMCQ 9DAC310D808E1AC3 zp2_human Zona pellucida sperm-binding protein 2 ZP2 ZPA Zona pellucida glycoprotein 2 Zona pellucida protein A protein protein human Homo sapiens Human MACRQRGGSWSPSGWFNAGWSTYRSISLFFALVTSGNSIDVSQLVNPAFPGTVTCDEREITVEFPSSPGTKKWHASVVDPLGLDMPNCTYILDPEKLTLRATYDNCTRRVHGGHQMTIRVMNNSAALRHGAVMYQFFCPAMQVEETQGLSASTICQKDFMSFSLPRVFSGLADDSKGTKVQMGWSIEVGDGARAKTLTLPEAMKEGFSLLIDNHRMTFHVPFNATGVTHYVQGNSHLYMVSLKLTFISPGQKVIFSSQAICAPDPVTCNATHMTLTIPEFPGKLKSVSFENQNIDVSQLHDNGIDLEATNGMKLHFSKTLLKTKLSEKCLLHQFYLASLKLTFLLRPETVSMVIYPECLCESPVSIVTGELCTQDGFMDVEVYSYQTQPALDLGTLRVGNSSCQPVFEAQSQGLVRFHIPLNGCGTRYKFEDDKVVYENEIHALWTDFPPSKISRDSEFRMTVKCSYSRNDMLLNINVESLTPPVASVKLGPFTLILQSYPDNSYQQPYGENEYPLVRFLRQPIYMEVRVLNRDDPNIKLVLDDCWATSTMDPDSFPQWNVVVDGCAYDLDNYQTTFHPVGSSVTHPDHYQRFDMKAFAFVSEAHVLSSLVYFHCSALICNRLSPDSPLCSVTCPVSSRHRRATGATEAEKMTVSLPGPILLLSDDSSFRGVGSSDLKASGSSGEKSRSETGEEVGSRGAMDTKGHKTAGDVGSKAVAAVAAFAGVVATLGFIYYLYEKRTVSNH 2614DA79738F2CDD zp2-zp2-1 1 6 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1a Negative staining indicated that all peptides self-assemble forming fibrous arrangements with the basic characteristics of amyloid fibrils, since they appear straight, long and unbranched with a tendency to coalesce laterally (Fig. 1). More specifically, the ‘aggregation-prone’ peptides HZP2_A and HZP3_G self-assemble into amyloid-like fibrils with a diameter of 30–50 Å that coalesce laterally forming striated ribbons of various thickness (Fig. 1A,D). The HZP2_G peptide forms amyloid-like fibrils with a diameter of 70–100 Å (Fig. 1B), whereas the HZP3_A, HZP4_A and HZP4_G peptides form superhelical arrangements composed of two to several individual fibrils that wound around each other, with diameters that vary between 70 and 120 Å, respectively (Fig. 1C,E,F) zp2-zp2-2 1 6 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1b Negative staining indicated that all peptides self-assemble forming fibrous arrangements with the basic characteristics of amyloid fibrils, since they appear straight, long and unbranched with a tendency to coalesce laterally (Fig. 1). More specifically, the ‘aggregation-prone’ peptides HZP2_A and HZP3_G self-assemble into amyloid-like fibrils with a diameter of 30–50 Å that coalesce laterally forming striated ribbons of various thickness (Fig. 1A,D). The HZP2_G peptide forms amyloid-like fibrils with a diameter of 70–100 Å (Fig. 1B), whereas the HZP3_A, HZP4_A and HZP4_G peptides form superhelical arrangements composed of two to several individual fibrils that wound around each other, with diameters that vary between 70 and 120 Å, respectively (Fig. 1C,E,F) zp2-zp2-3 1 4 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1c Negative staining indicated that all peptides self-assemble forming fibrous arrangements with the basic characteristics of amyloid fibrils, since they appear straight, long and unbranched with a tendency to coalesce laterally (Fig. 1). More specifically, the ‘aggregation-prone’ peptides HZP2_A and HZP3_G self-assemble into amyloid-like fibrils with a diameter of 30–50 Å that coalesce laterally forming striated ribbons of various thickness (Fig. 1A,D). The HZP2_G peptide forms amyloid-like fibrils with a diameter of 70–100 Å (Fig. 1B), whereas the HZP3_A, HZP4_A and HZP4_G peptides form superhelical arrangements composed of two to several individual fibrils that wound around each other, with diameters that vary between 70 and 120 Å, respectively (Fig. 1C,E,F) zp2-zp3-1 1 4 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1d Negative staining indicated that all peptides self-assemble forming fibrous arrangements with the basic characteristics of amyloid fibrils, since they appear straight, long and unbranched with a tendency to coalesce laterally (Fig. 1). More specifically, the ‘aggregation-prone’ peptides HZP2_A and HZP3_G self-assemble into amyloid-like fibrils with a diameter of 30–50 Å that coalesce laterally forming striated ribbons of various thickness (Fig. 1A,D). The HZP2_G peptide forms amyloid-like fibrils with a diameter of 70–100 Å (Fig. 1B), whereas the HZP3_A, HZP4_A and HZP4_G peptides form superhelical arrangements composed of two to several individual fibrils that wound around each other, with diameters that vary between 70 and 120 Å, respectively (Fig. 1C,E,F) zp2-zp3-2 1 5 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1e Negative staining indicated that all peptides self-assemble forming fibrous arrangements with the basic characteristics of amyloid fibrils, since they appear straight, long and unbranched with a tendency to coalesce laterally (Fig. 1). More specifically, the ‘aggregation-prone’ peptides HZP2_A and HZP3_G self-assemble into amyloid-like fibrils with a diameter of 30–50 Å that coalesce laterally forming striated ribbons of various thickness (Fig. 1A,D). The HZP2_G peptide forms amyloid-like fibrils with a diameter of 70–100 Å (Fig. 1B), whereas the HZP3_A, HZP4_A and HZP4_G peptides form superhelical arrangements composed of two to several individual fibrils that wound around each other, with diameters that vary between 70 and 120 Å, respectively (Fig. 1C,E,F) zp4-zp4-1 1 5 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f1f Negative staining indicated that all peptides self-assemble forming fibrous arrangements with the basic characteristics of amyloid fibrils, since they appear straight, long and unbranched with a tendency to coalesce laterally (Fig. 1). More specifically, the ‘aggregation-prone’ peptides HZP2_A and HZP3_G self-assemble into amyloid-like fibrils with a diameter of 30–50 Å that coalesce laterally forming striated ribbons of various thickness (Fig. 1A,D). The HZP2_G peptide forms amyloid-like fibrils with a diameter of 70–100 Å (Fig. 1B), whereas the HZP3_A, HZP4_A and HZP4_G peptides form superhelical arrangements composed of two to several individual fibrils that wound around each other, with diameters that vary between 70 and 120 Å, respectively (Fig. 1C,E,F) zp2-zp2-4 2 6 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2a X-ray diffraction experiments were performed on fibers containing amyloid-like fibrils, derived by self-assembly of each ‘aggregation-prone’ peptide. The X-ray diffraction patterns indicate that amyloid fibrils formed in every case possess the typical ‘cross-β’-like architecture of amyloid fibrils (Fig. 2). zp2-zp2-5 2 6 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2b X-ray diffraction experiments were performed on fibers containing amyloid-like fibrils, derived by self-assembly of each ‘aggregation-prone’ peptide. The X-ray diffraction patterns indicate that amyloid fibrils formed in every case possess the typical ‘cross-β’-like architecture of amyloid fibrils (Fig. 2). zp3-zp3-1 2 4 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2c X-ray diffraction experiments were performed on fibers containing amyloid-like fibrils, derived by self-assembly of each ‘aggregation-prone’ peptide. The X-ray diffraction patterns indicate that amyloid fibrils formed in every case possess the typical ‘cross-β’-like architecture of amyloid fibrils (Fig. 2). zp3-zp3-2 2 4 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2d X-ray diffraction experiments were performed on fibers containing amyloid-like fibrils, derived by self-assembly of each ‘aggregation-prone’ peptide. The X-ray diffraction patterns indicate that amyloid fibrils formed in every case possess the typical ‘cross-β’-like architecture of amyloid fibrils (Fig. 2). zp4-zp4-2 2 5 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2e X-ray diffraction experiments were performed on fibers containing amyloid-like fibrils, derived by self-assembly of each ‘aggregation-prone’ peptide. The X-ray diffraction patterns indicate that amyloid fibrils formed in every case possess the typical ‘cross-β’-like architecture of amyloid fibrils (Fig. 2). zp4-zp4-3 2 5 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f2f X-ray diffraction experiments were performed on fibers containing amyloid-like fibrils, derived by self-assembly of each ‘aggregation-prone’ peptide. The X-ray diffraction patterns indicate that amyloid fibrils formed in every case possess the typical ‘cross-β’-like architecture of amyloid fibrils (Fig. 2). zp2-zp2-6 3 6 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3a t1 ATR FT-IR spectra obtained from thin hydrated films containing amyloid-like fibrils from the solution samples of the ‘aggregation-prone’ peptides indicate that they adopt an antiparallel β-sheet conformation, supporting our X-ray diffraction results (Fig. 3). More specifically, a preponderant amide I β-sheet band is viewed for the HZP2_A, HZP2_G, HZP3_A, HZP3_G, HZP4_A and HZP4_G peptides (Table 1), whereas similar assignments arise based on the presence of an amide II peak, viewed for spectra derived from all peptides, respectively. zp2-zp2-7 3 6 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3b t1 ATR FT-IR spectra obtained from thin hydrated films containing amyloid-like fibrils from the solution samples of the ‘aggregation-prone’ peptides indicate that they adopt an antiparallel β-sheet conformation, supporting our X-ray diffraction results (Fig. 3). More specifically, a preponderant amide I β-sheet band is viewed for the HZP2_A, HZP2_G, HZP3_A, HZP3_G, HZP4_A and HZP4_G peptides (Table 1), whereas similar assignments arise based on the presence of an amide II peak, viewed for spectra derived from all peptides, respectively. Finally, an additional shoulder determined by the second derivative spectra (Fig. S3), located in the 1690–1697 cm−1 region in all cases, suggests that the peptides form antiparallel β-sheets (Table 1). zp3-zp3-3 3 4 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3c t1 ATR FT-IR spectra obtained from thin hydrated films containing amyloid-like fibrils from the solution samples of the ‘aggregation-prone’ peptides indicate that they adopt an antiparallel β-sheet conformation, supporting our X-ray diffraction results (Fig. 3). More specifically, a preponderant amide I β-sheet band is viewed for the HZP2_A, HZP2_G, HZP3_A, HZP3_G, HZP4_A and HZP4_G peptides (Table 1), whereas similar assignments arise based on the presence of an amide II peak, viewed for spectra derived from all peptides, respectively. Finally, an additional shoulder determined by the second derivative spectra (Fig. S3), located in the 1690–1697 cm−1 region in all cases, suggests that the peptides form antiparallel β-sheets (Table 1). zp3-zp3-4 3 4 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3d t1 ATR FT-IR spectra obtained from thin hydrated films containing amyloid-like fibrils from the solution samples of the ‘aggregation-prone’ peptides indicate that they adopt an antiparallel β-sheet conformation, supporting our X-ray diffraction results (Fig. 3). More specifically, a preponderant amide I β-sheet band is viewed for the HZP2_A, HZP2_G, HZP3_A, HZP3_G, HZP4_A and HZP4_G peptides (Table 1), whereas similar assignments arise based on the presence of an amide II peak, viewed for spectra derived from all peptides, respectively. Finally, an additional shoulder determined by the second derivative spectra (Fig. S3), located in the 1690–1697 cm−1 region in all cases, suggests that the peptides form antiparallel β-sheets (Table 1). zp4-zp4-4 3 5 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3e t1 ATR FT-IR spectra obtained from thin hydrated films containing amyloid-like fibrils from the solution samples of the ‘aggregation-prone’ peptides indicate that they adopt an antiparallel β-sheet conformation, supporting our X-ray diffraction results (Fig. 3). More specifically, a preponderant amide I β-sheet band is viewed for the HZP2_A, HZP2_G, HZP3_A, HZP3_G, HZP4_A and HZP4_G peptides (Table 1), whereas similar assignments arise based on the presence of an amide II peak, viewed for spectra derived from all peptides, respectively. Finally, an additional shoulder determined by the second derivative spectra (Fig. S3), located in the 1690–1697 cm−1 region in all cases, suggests that the peptides form antiparallel β-sheets (Table 1). zp4-zp4-5 3 5 unspecified role unspecified role neutral component neutral component purified purified binding range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role neutral component neutral component purified purified bindind range binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction f3f t1 ATR FT-IR spectra obtained from thin hydrated films containing amyloid-like fibrils from the solution samples of the ‘aggregation-prone’ peptides indicate that they adopt an antiparallel β-sheet conformation, supporting our X-ray diffraction results (Fig. 3). More specifically, a preponderant amide I β-sheet band is viewed for the HZP2_A, HZP2_G, HZP3_A, HZP3_G, HZP4_A and HZP4_G peptides (Table 1), whereas similar assignments arise based on the presence of an amide II peak, viewed for spectra derived from all peptides, respectively. Finally, an additional shoulder determined by the second derivative spectra (Fig. S3), located in the 1690–1697 cm−1 region in all cases, suggests that the peptides form antiparallel β-sheets (Table 1).