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 Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. (0014-5793) 2013 Fisher OS., Zhang R., Li X., Murphy JW., Demeler B., Boggon TJ. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction experimental particp experimental participant identification experimental particp Fisher OS., Zhang R., Li X., Murphy JW., Demeler B., Boggon TJ. FEBS Lett. (0014-5793) 2013 Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. (0014-5793) 2013 Fisher OS., Zhang R., Li X., Murphy JW., Demeler B., Boggon TJ. in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Fisher OS., Zhang R., Li X., Murphy JW., Demeler B., Boggon TJ. FEBS Lett. (0014-5793) 2013 ccm2_human Cerebral cavernous malformations 2 protein CCM2 C7orf22 Malcavernin PP10187 protein protein human Homo sapiens Human MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA 43F9C153B4DE460E pdc10_human Programmed cell death protein 10 PDCD10 CCM3 TFAR15 TF-1 cell apoptosis-related protein 15 Cerebral cavernous malformations 3 protein protein protein human Homo sapiens Human MRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIIMKILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIPDEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKAINVFVSANRLIHQTNLILQTFKTVA DIP protein Q9BUL8 original sequence version: 96 DIP protein Q9BUL8 original sequence version: 125 5AA613F71FAAEF56 ccm2-pdcd10 2 CCM2 3 weight by comassie molecular weight estimation by coomasie staining weight by comassie experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined CCM3 4 weight by comassie molecular weight estimation by coomasie staining weight by comassie experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey purified purified direct interaction direct interaction f1d homomint mint The CCM2 C-terminal domain does not interact with CCM3. ccm2-1 1 CCM2 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp 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 his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 4.0 direct interaction direct interaction mint The structure is deposited in the PDB with accession code 4FQN. f2a f2b f2c f3 st1 sf1 We therefore determined its structure by X-ray crystallography by using the SAD method (Fig S1), and refined against a 1.9Å native dataset (Table S1). Overall, we found good electron density throughout the structure (Fig S1), with four copies of CCM2 per asymmetric unit.The CCM2 HHD crystallizes with four copies per asymmetric unit. Analysis of the crystal packing reveals two distinct conformations. Two of the copies (chains A and B) have an extensive interaction interface between them (Fig 3A), but this interface is not observed for the other two copies (chains C and D) either in the asymmetric unit or with symmetry-related molecules.