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 H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. EMBO J. (0261-4189) 2002 Ha Y., Stevens DJ., Skehel JJ., Wiley DC. Virus - Publications including interactions involving viral proteins no in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Ha Y., Stevens DJ., Skehel JJ., Wiley DC. Virus - Publications including interactions involving viral proteins no EMBO J. (0261-4189) 2002 hema_i83a4 Hemagglutinin HA protein protein i83a4 Influenza A virus (strain A/Turkey/Ireland/1378/1983 H5N8) MEKIVLLFAIVSLVRSDQICIGYHANNSTKQVDTIMEKNVTVTHAQDILEKTHNGKLCSLNGVKPLILRDCSVAGWLLGNPMCDEFLNVPEWSYIVEKDNPVNGLCYPGDFNDYEELKHLLSCTKHFEKIRIIPRDSWPNHEASLGVSSACPYNGRSSFFRNVVWLIKKNNAYPTIKRSYSNTNKEDLLILWGIHHPNDAAEQTKLYQNPTTYVSVGTSTLNQRSIPKIATRPELNGQSGRMEFFWTILKPSDTINFESNGNFIAPEYAYKIVKKGDSAIMKSGLEYGNCNTKCQTPIGAINSSMPLHNIHPLTIGECPKYVKSDRLVLATGLRNTPQRKRKKRGLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQRAIDGITNKVNSIIDKMNTQFEAVGKEFNNLERRIENLNKKMEDGFLDVWTYNAELLVLMENERTLDFHDANVKSLYDKVRLQLKDNARELGNGCFEFYHKCDNECMESIRNGTYNYPQYSEEARLNREEISGVKLESMGIYQILSIYSTVASSLALAIMIAGLSFWMCSNGSLQCRICI mint 29D16ECC76D5D03B hema_i87a1 Hemagglutinin HA protein protein i87a1 Influenza A virus (strain A/Mallard/Ohio/556/1987 H5N9) MERIVIALAIINIVKGDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKEHNGKLCSLKGVRPLILKDCSVAGWLLGNPMCDEFLNVPEWSYIVEKDNPVNGLCYPGDFNDYEELKHLMSSTNHFEKIQIIPRNSWSTHDASSGVSSACPYNGRSSFFRNVVWLIKKNNAYPTIKRTYNNTNVEDLLILWGIHHPNDAAEQTKLYQNSNTYVSVGTSTLNQRSIPEIATRPKVNGQSGRMEFFWTILRPNDAISFESNGNFIAPEYAYKIVKKGDSAIMKSELEYGNCDTKCQTPVGAINSSMPFHNVHPLTIGECPKYVKSDKLVLATGLRNVPQRETRGLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGITNKVNSIIDKMNTQFEAVGKEFNNLERRIENLNKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYPQYSEESRLNREEIDGVKLESMGTYQILSIYSTVASSLALAIMVAGLSFWMCSNGSLQCRICI mint Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore 8DD897621EE1B929 ha-ha 1 HEMA 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 HEMA 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1jsm, P11135 is chain A and P87506 is chain B Resolution 1.900 homomint mint