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 Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy. Influence of inflammation-related changes on conformational characteristics of HLA-B27 subtypes as detected by IR spectroscopy. FEBS J. (1742-464X) 2011 imex curation Fabian H., Loll B., Huser H., Naumann D., Uchanska-Ziegler B., Ziegler A. Only protein-protein interactions in vitro In vitro biophysical biophysical predetermined predetermined participant predetermined Fabian H., Loll B., Huser H., Naumann D., Uchanska-Ziegler B., Ziegler A. FEBS J. (1742-464X) 2011 Only protein-protein interactions imex curation 1a68_human HLA class I histocompatibility antigen, A-68 alpha chain HLA-A HLAA Aw-68 HLA class I histocompatibility antigen, A-28 alpha chain MHC class I antigen A*68 protein protein human Homo sapiens Human MAVMAPRTLVLLLSGALALTQTWAGSHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDRNTRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQMMYGCDVGSDGRFLRGYRQDAYDGKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQWRAYLEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWVAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEPSSQPTIPIVGIIAGLVLFGAVITGAVVAAVMWRRKSSDRKGGSYSQAASSDSAQGSDVSLTACKV 78539C59DB8B1DFC vipr1_human Vasoactive intestinal polypeptide receptor 1 VIPR1 Pituitary adenylate cyclase-activating polypeptide type II receptor VPAC1 protein protein human Homo sapiens Human MRPPSPLPARWLCVLAGALAWALGPAGGQAARLQEECDYVQMIEVQHKQCLEEAQLENETIGCSKMWDNLTCWPATPRGQVVVLACPLIFKLFSSIQGRNVSRSCTDEGWTHLEPGPYPIACGLDDKAASLDEQQTMFYGSVKTGYTIGYGLSLATLLVATAILSLFRKLHCTRNYIHMHLFISFILRAAAVFIKDLALFDSGESDQCSEGSVGCKAAMVFFQYCVMANFFWLLVEGLYLYTLLAVSFFSERKYFWGYILIGWGVPSTFTMVWTIARIHFEDYGCWDTINSSLWWIIKGPILTSILVNFILFICIIRILLQKLRPPDIRKSDSSPYSRLARSTLLLIPLFGVHYIMFAFFPDNFKPEVKMVFELVVGSFQGFVVAILYCFLNGEVQAELRRKWRRWHLQGVLGWNPKYRHPSGGSNGATCSTQVSMLTRVSPGARRSSSFQAEVSLV DAA40CF5BEC47D7D hla_b-vipr1 1 B*27 2 predetermined predetermined participant predetermined 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 VIPR 3 peptide synthesis peptide synthesis predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component in vitro translated in vitro translated protein in vitro translated binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction homomint mint f2 f3 f4 f5 t1 sf1 infrared spectroscopy (MI:0964) study with the extra-cellular domains of B*2705 and B*2709 as well as 13C-labeled beta2m in complex with citrulline-modified peptide pVIPR-U5 (RRKWURWHL; U = citrulline) and nonapeptide pVIPR. The IR data of B*2709/13C-beta2m:pVIPR and B*2705/13C-beta2m:pVIPR are from previous work by our group [27].