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 Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment. Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment. FEBS J. (1742-464X) 2011 imex curation Liao TY., Lee LY., Chen RP. Only protein-protein interactions in vitro In vitro cd circular dichroism CD CD cd peptide synthesis peptide synthesis Liao TY., Lee LY., Chen RP. FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment. Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment. FEBS J. (1742-464X) 2011 imex curation Liao TY., Lee LY., Chen RP. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy peptide synthesis peptide synthesis Liao TY., Lee LY., Chen RP. FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment. Leu138 in bovine prion peptide fibrils is involved in seeding discrimination related to codon 129 M/V polymorphism in the prion peptide seeding experiment. FEBS J. (1742-464X) 2011 imex curation Liao TY., Lee LY., Chen RP. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence peptide synthesis peptide synthesis Liao TY., Lee LY., Chen RP. FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation prio_human Major prion protein PrP27-30 PrP33-35C ASCR PRNP PRIP PRP ALTPRP protein protein human Homo sapiens Human MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG DIP protein P04156 original sequence version: 125 DIP protein P04156 original sequence version: 122 DIP protein P04156 original sequence version: 147 DIP protein P04156 original sequence version: 141 DIP protein P04156 original sequence version: 166 DIP protein P04156-1 original sequence version: 166 43DB596BAAA66484 prio_bovin Major prion protein PRNP PRP Major scrapie-associated fibril protein 1 protein protein bovin Bos taurus (Bovine) Bovine MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG The function of PrP is not known. PrP is encoded in the host genome and is expressed both in normal and infected cells Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc mint homomint D6D214038316A231 prnp-1 2 huPrP 4 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association mint f2b f2c f2d No clear difference in morphology can be concluded based on these image except that huPrP129V fibrils did not favor lateral association compared with the other three. prnp-1 2 PrP 5 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association f2a mint prnp-1 3 huPrP 4 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association mint It should be noted that the emitted ThT fluorescence was particularly high for the huPrP129V peptide (note the different scale for the y axis for this peptide). We surmise that the big difference in ThT fluorescence emission might be because (1) the position 129 is in the ThT binding site and Val-129 favors ThT binding; (2) the position 129 is involved in the ThT binding interface and Val-129 increases ThT fluorescence quantum yield; (3) Val-129 affects fibril assembly which affects ThT binding. f1b f3b f3c prnp-1 3 bPrP 5 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association mint f1b f3a prnp-1 1 huPrP 4 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association f1a mint prnp-1 1 bPrP 5 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association mint f1a f4a t3 prnp-prnp-18 1 bPrP 5 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain huPrP 4 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P04156:p.Met129Val mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain M V Tue Jul 12 10:09:58 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:34:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met129val' Tue Jun 30 18:46:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met129Val' association association homomint mint As shown in Figure 4B, the minimal bPrP seed amount required to efficiently seed the bPrP, huPrP129M, huPrP129M/V, and huPrP129V peptide solutions was 1, 2, 10, and 20 %, respectively. Clearly, bPrP amyloid was more efficient at seeding the huPrP129M peptide than the huPrP129V and huPrP129M/V peptides. According to our peptide model, the normalized seeding efficiency of the bPrP seed was 1/1 : 1/2 : 1/10 : 1/20 or 1 : 0.5 : 0.1 : 0.05 for bPrP, huPrP129M, huPrP129M/V, and huPrP129V. The Met-129→Val substitution resulted in a 10- fold lower seeding efficiency for bPrP seeds. f4 t3 prnp-prnp-19 1 bPrP 5 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P10279:p.Leu149Ile mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain L I Tue Jul 12 10:07:47 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:19:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu149ile' Tue Jun 30 16:50:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu149Ile' huPrP 4 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association homomint mint The seeding efficiencies of the V112M, L138I, and N143S seeds for the bPrP, huPrP129M, huPrP129M/V, and huPrP129V monomer were shown in Figure S2. For clarity, the data are summarized and compared with the bPrP seeding results (Figure 3) in Table 3. The normalized seeding efficiency of the V112M seed was 1 : 0.5 : 0.1 : 0.05 for bPrP, huPrP129M, huPrP129M/V, and huPrP129V. This result is the same as that of the bPrP seed. These data suggested that the fibrils formed from V112M are very similar to those formed from bPrP and that the Val-112→Met mutation is not involved in the interference effect. Interestingly, the normalized seeding efficiency of the L138I seed was 1 : 0.5 : 0.25 for huPrP129M, huPrP129M/V and huPrP129V. This result is the same as that of the huPrP129M seed. When L138I fibrils were used as seeds, huPrP129V had no interference effect in the huPrP129M/V mixture. These data suggested that Leu-138 in the bovine PrP peptide is the residue responsible for the interference effect of huPrP129V in the huPrP129M and huPrP129V mixture and for the large seeding barrier in seeding huPrP129V. t3 sf2