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 Dynamics and allosteric potential of the AMPA receptor N-terminal domain. Dynamics and allosteric potential of the AMPA receptor N-terminal domain. EMBO J. (0261-4189) 2011 imex curation Sukumaran M., Rossmann M., Shrivastava I., Dutta A., Bahar I., Greger IH. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Sukumaran M., Rossmann M., Shrivastava I., Dutta A., Bahar I., Greger IH. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation gria3_rat Glutamate receptor 3 Gria3 Glur3 GluR-K3 Glutamate receptor ionotropic, AMPA 3 AMPA-selective glutamate receptor 3 GluR-C protein protein rat Rattus norvegicus (Rat) Rat MGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLSYYKWEKFVYLYDTERGFSVLQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSSSSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI DIP protein P19492 original sequence version: 141 2981616375661703 gria3-1 1 GluA3 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 Stoichiometry: 2.0 direct interaction direct interaction mint st1 st2 f2 sf3 sf4 f3 GluA3 NTD crystals diffracted to 2.2A° . The structure was solved by molecular replacement using GluA2 (PDB 3HSY; Greger et al, 2009) as a search probe; two dimers (I and II) are present in the asymmetric unit (Supplementary Table I)...Overall, the three alternative quaternary conformations I, II and III provide examples of dimeric rearrangements that are energetically accessible to the GluA3 NTD. Coordinates for WT GluA2 (3HSY), GluA2-T78A (3N6V) and GluA2-N54A (3O2J) were deposited in the Protein Data Bank.