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 http://mint.bio.uniroma2.it/mint anonymous-2014n-1 Structural basis for the specific recognition of IL-18 by its alpha receptor in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined xinquanwang@mail.tsinghua.edu.cn 2014 imex curation Wei H., Wang D., Qian Y., Liu X., Fan S., Yin H.S., Wang X. FEBS Lett. (0014-5793) Only protein-protein interactions anonymous-2014g-2 Structural basis for the specific recognition of IL-18 by its alpha receptor in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie xinquanwang@mail.tsinghua.edu.cn 2014 imex curation Wei H., Wang D., Qian Y., Liu X., Fan S., Yin H.S., Wang X. FEBS Lett. (0014-5793) Only protein-protein interactions il18r_human Interleukin-18 receptor 1 Interleukin-18 receptor alpha IL18R1 IL1RRP CD218 antigen-like family member A CDw218a IL1 receptor-related protein protein protein human Homo sapiens Human MNCRELPLTLWVLISVSTAESCTSRPHITVVEGEPFYLKHCSCSLAHEIETTTKSWYKSSGSQEHVELNPRSSSRIALHDCVLEFWPVELNDTGSYFFQMKNYTQKWKLNVIRRNKHSCFTERQVTSKIVEVKKFFQITCENSYYQTLVNSTSLYKNCKKLLLENNKNPTIKKNAEFEDQGYYSCVHFLHHNGKLFNITKTFNITIVEDRSNIVPVLLGPKLNHVAVELGKNVRLNCSALLNEEDVIYWMFGEENGSDPNIHEEKEMRIMTPEGKWHASKVLRIENIGESNLNVLYNCTVASTGGTDTKSFILVRKADMADIPGHVFTRGMIIAVLILVAVVCLVTVCVIYRVDLVLFYRHLTRRDETLTDGKTYDAFVSYLKECRPENGEEHTFAVEILPRVLEKHFGYKLCIFERDVVPGGAVVDEIHSLIEKSRRLIIVLSKSYMSNEVRYELESGLHEALVERKIKIILIEFTPVTDFTFLPQSLKLLKSHRVLKWKADKSLSYNSRFWKNLLYLMPAKTVKPGRDEPEVLPVLSES il18_human Interleukin-18 IL18 IGIF IL1F4 Iboctadekin Interferon gamma-inducing factor Interleukin-1 gamma protein protein human Homo sapiens Human MAAEPVEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED il18-il18r1 1567449 n/a IL-18R alpha 1567451 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a IL-18 1567452 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false t1 f1 f3 f4 sf2 The final model in the asymmetric unit contains two IL-18-IL-18Rα complexes (Figure S2A), with residues Tyr1-Asn155 in IL-18 and residues Ser21-Cys43, Thr51-Arg71, Arg75-Leu161, Pro169-GLu253, and Asn260-Asp318 in IL-18Rα. il18-il18r1-1 1567450 n/a IL-18 1567452 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a IL-18R alpha 1567451 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false sf1b The purified IL-18 (residues Tyr1-Asp157) bound to human IL-18Rα ectodomain (residues Ala19-Arg329), which was expressed and purified from insect cells, to form the IL-18-IL-18Rα complex (Figure S1B).