DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Chaudhry C., Plested AJ., Schuck P., Mayer ML. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Chaudhry C., Plested AJ., Schuck P., Mayer ML. DIP original experiment: DIP-260369X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Chaudhry C., Plested AJ., Schuck P., Mayer ML. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Chaudhry C., Plested AJ., Schuck P., Mayer ML. DIP original experiment: DIP-260368X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Chaudhry C., Plested AJ., Schuck P., Mayer ML. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Chaudhry C., Plested AJ., Schuck P., Mayer ML. DIP original experiment: DIP-260370X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Chaudhry C., Plested AJ., Schuck P., Mayer ML. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Chaudhry C., Plested AJ., Schuck P., Mayer ML. DIP original experiment: DIP-260371X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. 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 grid2_rat Glutamate receptor ionotropic, delta-2 Grid2 protein protein rat Rattus norvegicus (Rat) Rat MEVFPLLFFLSFWWSRTWDLATSDSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKSLAGVFCILAAGIVLSCLIAVLETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFTFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI DIP protein Q63226 original sequence version: 71 DIP protein Q63226 original sequence version: 117 mint Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists 6583C31357C9402C grik2_rat Glutamate receptor ionotropic, kainate 2 Grik2 Glur6 Glutamate receptor 6 protein protein rat Rattus norvegicus (Rat) Rat MKIISPVLSNLVFSRSIKVLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA DIP protein P42260 original sequence version: 67 DIP protein P42260 original sequence version: 126 DIP protein P42260 original sequence version: 95 DIP protein P42260 original sequence version: 130 DIP protein P42260 original sequence version: 106 DIP protein P42260 original sequence version: 134 DIP protein P42260 original sequence version: 124 mint 7F430E2D8B2E982B grik2-8 4 7 unspecified role unspecified role unspecified role unspecified role Region 429-806 Region 429-806 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction gria2-1 2 5 unspecified role unspecified role unspecified role unspecified role Region 413-796 Region 413-796 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction gria2-3 1 5 unspecified role unspecified role unspecified role unspecified role Region 413-796 Region 413-796 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction grid2-2 3 6 unspecified role unspecified role unspecified role unspecified role Region 440-551/664-813 Region 440-551/664-813 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction