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 Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. EMBO J. (0261-4189) 2011 imex curation Rossmann M., Sukumaran M., Penn AC., Veprintsev DB., Babu MM., Greger IH. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rossmann M., Sukumaran M., Penn AC., Veprintsev DB., Babu MM., Greger IH. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. EMBO J. (0261-4189) 2011 imex curation Rossmann M., Sukumaran M., Penn AC., Veprintsev DB., Babu MM., 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 Rossmann M., Sukumaran M., Penn AC., Veprintsev DB., Babu MM., Greger IH. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. EMBO J. (0261-4189) 2011 imex curation Rossmann M., Sukumaran M., Penn AC., Veprintsev DB., Babu MM., Greger IH. Only protein-protein interactions in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Rossmann M., Sukumaran M., Penn AC., Veprintsev DB., Babu MM., Greger IH. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation gria1_rat Glutamate receptor 1 Gria1 GluR-A GluR-K1 Glutamate receptor ionotropic, AMPA 1 AMPA-selective glutamate receptor 1 Glur1 protein protein rat Rattus norvegicus (Rat) Rat MPYIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQEALISIIDHYKWQTFVYIYDADRGLSVLQRVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPARIMQQWRTSDSRDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASGGGGSGENGRVVSQDFPKSMQSIPCMSHSSGMPLGATGL DIP protein P19490 original sequence version: 146 DIP protein P19490 original sequence version: 142 DIP protein P19490 original sequence version: 117 DIP protein P19490 original sequence version: 127 DIP protein P19490 original sequence version: 131 DIP protein P19490 original sequence version: 129 2D4CFA7CCD532838 gria2_rat Glutamate receptor 2 Gria2 Glur2 GluR-B GluR-K2 Glutamate receptor ionotropic, AMPA 2 AMPA-selective glutamate receptor 2 protein protein rat Rattus norvegicus (Rat) Rat MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI DIP protein P19491 original sequence version: 164 DIP protein P19491 original sequence version: 160 DIP protein P19491 original sequence version: 131 DIP protein P19491 original sequence version: 136 DIP protein P19491 original sequence version: 141 DEFA817027C1CCD1 gria4_rat Glutamate receptor 4 Gria4 Glur4 GluR-D Glutamate receptor ionotropic, AMPA 4 AMPA-selective glutamate receptor 4 protein protein rat Rattus norvegicus (Rat) Rat MRIICRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDMPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYTEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEATRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP DIP protein P19493 original sequence version: 125 mint Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist homomint 873D1B4C710C4459 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 gria2-2 1 GluA2 5 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 f1a t1 sf1 sf4b gria2-2 1 GluA2 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P19491:p.Thr99Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T A Tue Jul 12 10:14:47 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 14:30:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr99ala' Tue Jun 30 17:14:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr99Ala' 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 f1a t1 sf1 sf4b gria2-2 1 GluA2 5 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 P19491:p.Asn75Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N A Tue Jul 12 10:11:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 17:26:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn75ala' Tue Jun 30 19:04:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn75Ala' Stoichiometry: 2.0 direct interaction direct interaction mint f1a t1 sf1 sf4b gria1-1 1 GluA1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint f1a t1 gria4-1 1 GluA4 6 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 f1a t1 gria1-gria2 1 GluA2 5 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 GluA1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint f1b t1 gria2-gria4 1 GluA4 6 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 GluA2 5 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 30 32 direct interaction direct interaction homomint mint t1 sf2d gria2-gria3 1 GluA3 7 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 GluA2 5 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 35 37 direct interaction direct interaction homomint mint f1b t1 sf2b gria1-gria3 1 GluA1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified GluA3 7 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 direct interaction direct interaction mint f1b t1 sf2a gria2-2 2 GluA2 5 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 The crystal structure of GluA2-T78A, solved to 3.2A° (Supplementary Table I; PDB 3N6V), revealed that the mutation induces intra- and inter-helical rotations in the fourhelical bundle of the UL (Supplementary Figure S5C, D), culminating in a rearranged interface with reduced contact area (approximately 1.4-fold reduced, solvent-accessible surface area). Therefore, alteration at position 78 in the core of the NTD interface facilitates heteromerization by destabilizing homodimeric contacts. Mutation of this core position likely weakens homodimers, increasing subunit availability for heteromeric assembly (Figure 6C, step I)...The crystal structure of GluA2-N54A solved to 1.95A° confirmed that the N54A mutation replaces this unsatisfied H-bond with a hydrophobic link (Figure 6A), resulting in a tighter, otherwise unaltered, homodimer (PDB 3O2J). This mutation likely stabilizes homo- and heterodimers (Table I; Figure 6C, step II). st1 f2b f2c sf5 f6a gria2-2 3 GluA2 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P19491:p.Thr99Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T A Tue Jul 12 10:56:12 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 17:48:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr99ala' Tue Jun 30 17:17:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr99Ala' 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 sf4a gria2-2 3 GluA2 5 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 P19491:p.Asn75Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N A Tue Jul 12 10:56:38 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:41:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn75ala' Tue Jun 30 16:47:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn75Ala' Stoichiometry: 2.0 direct interaction direct interaction mint sf4a