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- SASDDY5: AMPA subtype ionotropic Glutamate receptor GluA2 in the resting s... -

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Basic information

Entry
Database: SASBDB / ID: SASDDY5
SampleAMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents
  • Glutamate receptor 2GRIA2 (protein), GluA2, Rattus norvegicus
Function / homology
Function and homology information


spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / response to lithium ion / perisynaptic space / cellular response to glycine / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / immunoglobulin binding ...spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / response to lithium ion / perisynaptic space / cellular response to glycine / AMPA glutamate receptor activity / Trafficking of GluR2-containing AMPA receptors / immunoglobulin binding / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / extracellularly glutamate-gated ion channel activity / asymmetric synapse / regulation of receptor recycling / Unblocking of NMDA receptors, glutamate binding and activation / glutamate receptor binding / positive regulation of synaptic transmission / glutamate-gated receptor activity / presynaptic active zone membrane / response to fungicide / regulation of synaptic transmission, glutamatergic / cellular response to brain-derived neurotrophic factor stimulus / somatodendritic compartment / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / ionotropic glutamate receptor binding / ionotropic glutamate receptor signaling pathway / dendrite cytoplasm / cytoskeletal protein binding / SNARE binding / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / dendritic shaft / synaptic membrane / synaptic transmission, glutamatergic / PDZ domain binding / postsynaptic density membrane / protein tetramerization / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / establishment of protein localization / terminal bouton / receptor internalization / synaptic vesicle membrane / cerebral cortex development / synaptic vesicle / presynapse / signaling receptor activity / presynaptic membrane / amyloid-beta binding / growth cone / perikaryon / chemical synaptic transmission / scaffold protein binding / postsynaptic membrane / dendritic spine / postsynaptic density / neuron projection / axon / neuronal cell body / dendrite / synapse / glutamatergic synapse / protein-containing complex binding / endoplasmic reticulum membrane / protein kinase binding / cell surface / endoplasmic reticulum / protein-containing complex / membrane / identical protein binding / plasma membrane
Similarity search - Function
Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. ...Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I
Similarity search - Domain/homology
Glutamate receptor 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Contact author
  • Andreas Larsen (University of Copenhagen, Copenhagen, Denmark)

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Structure visualization

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Models

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Sample

SampleName: AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents
Specimen concentration: 0.34 mg/ml
BufferName: D2O based buffer. 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O)
pH: 7.5
Entity #1037Name: GluA2 / Type: protein / Description: Glutamate receptor 2GRIA2 / Formula weight: 367.694 / Num. of mol.: 1 / Source: Rattus norvegicus / References: UniProt: P19491
Sequence: NSIQIGGLFP RGADQEYSAF RVGMVQFSTS EFRLTPHIDN LEVANSFAVT NAFCSQFSRG VYAIFGFYDK KSVNTITSFC GTLHVSFITP SFPTDGTHPF VIQMRPDLKG ALLSLIEYYQ WDKFAYLYDS DRGLSTLQAV LDSAAEKKWQ VTAINVGNIN NDKKDETYRS ...Sequence:
NSIQIGGLFP RGADQEYSAF RVGMVQFSTS EFRLTPHIDN LEVANSFAVT NAFCSQFSRG VYAIFGFYDK KSVNTITSFC GTLHVSFITP SFPTDGTHPF VIQMRPDLKG ALLSLIEYYQ WDKFAYLYDS DRGLSTLQAV LDSAAEKKWQ VTAINVGNIN NDKKDETYRS LFQDLELKKE RRVILDCERD KVNDIVDQVI TIGKHVKGYH YIIANLGFTD GDLLKIQFGG AEVSGFQIVD YDDSLVSKFI ERWSTLEEKE YPGAHTATIK YTSALTYDAV QVMTEAFRNL RKQRIEISRR GNAGDCLANP AVPWGQGVEI ERALKQVQVE GLSGNIKFDQ NGKRINYTIN IMELKTNGPR KIGYWSEVDK MVLTEDDTSG LEQKTVVVTT ILESPYVMMK ANHAALAGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF SLGAFMQQGA DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGTPVNLA VLKLSEQGLL DKLKNKWWYD KGECGAKDSG SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKGLV PRGNSIQIGG LFPRGADQEY SAFRVGMVQF STSEFRLTPH IDNLEVANSF AVTNAFCSQF SRGVYAIFGF YDKKSVNTIT SFCGTLHVSF ITPSFPTDGT HPFVIQMRPD LKGALLSLIE YYQWDKFAYL YDSDRGLSTL QAVLDSAAEK KWQVTAINVG NINNDKKDET YRSLFQDLEL KKERRVILDC ERDKVNDIVD QVITIGKHVK GYHYIIANLG FTDGDLLKIQ FGGAEVSGFQ IVDYDDSLVS KFIERWSTLE EKEYPGAHTA TIKYTSALTY DAVQVMTEAF RNLRKQRIEI SRRGNAGDCL ANPAVPWGQG VEIERALKQV QVEGLSGNIK FDQNGKRINY TINIMELKTN GPRKIGYWSE VDKMVLTEDD TSGLEQKTVV VTTILESPYV MMKANHAALA GNERYEGYCV DLAAEIAKHC GFKYKLTIVG DGKYGARDAD TKIWNGMVGE LVYGKADIAI APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHTEEF EDGRETQSSE STNEFGIFNS LWFSLGAFMQ QGADISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLSKQTEIA YGTLDSGSTK EFFRRSKIAV FDKMWTYMRS AEPSVFVRTT AEGVARVRKS KGKYAYLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSSLGTPV NLAVLKLSEQ GLLDKLKNKW WYDKGECGAK DSGSKEKTSA LSLSNVAGVF YILVGGLGLA MLVALIEFCY KSRAEAKRMK GLVPRGNSIQ IGGLFPRGAD QEYSAFRVGM VQFSTSEFRL TPHIDNLEVA NSFAVTNAFC SQFSRGVYAI FGFYDKKSVN TITSFCGTLH VSFITPSFPT DGTHPFVIQM RPDLKGALLS LIEYYQWDKF AYLYDSDRGL STLQAVLDSA AEKKWQVTAI NVGNINNDKK DETYRSLFQD LELKKERRVI LDCERDKVND IVDQVITIGK HVKGYHYIIA NLGFTDGDLL KIQFGGAEVS GFQIVDYDDS LVSKFIERWS TLEEKEYPGA HTATIKYTSA LTYDAVQVMT EAFRNLRKQR IEISRRGNAG DCLANPAVPW GQGVEIERAL KQVQVEGLSG NIKFDQNGKR INYTINIMEL KTNGPRKIGY WSEVDKMVLT EDDTSGLEQK TVVVTTILES PYVMMKANHA ALAGNERYEG YCVDLAAEIA KHCGFKYKLT IVGDGKYGAR DADTKIWNGM VGELVYGKAD IAIAPLTITL VREEVIDFSK PFMSLGISIM IKKPQKSKPG VFSFLDPLAY EIWMCIVFAY IGVSVVLFLV SRFSPYEWHT EEFEDGRETQ SSESTNEFGI FNSLWFSLGA FMQQGADISP RSLSGRIVGG VWWFFTLIII SSYTANLAAF LTVERMVSPI ESAEDLSKQT EIAYGTLDSG STKEFFRRSK IAVFDKMWTY MRSAEPSVFV RTTAEGVARV RKSKGKYAYL LESTMNEYIE QRKPCDTMKV GGNLDSKGYG IATPKGSSLG TPVNLAVLKL SEQGLLDKLK NKWWYDKGEC GAKDSGSKEK TSALSLSNVA GVFYILVGGL GLAMLVALIE FCYKSRAEAK RMKGLVPRGN SIQIGGLFPR GADQEYSAFR VGMVQFSTSE FRLTPHIDNL EVANSFAVTN AFCSQFSRGV YAIFGFYDKK SVNTITSFCG TLHVSFITPS FPTDGTHPFV IQMRPDLKGA LLSLIEYYQW DKFAYLYDSD RGLSTLQAVL DSAAEKKWQV TAINVGNINN DKKDETYRSL FQDLELKKER RVILDCERDK VNDIVDQVIT IGKHVKGYHY IIANLGFTDG DLLKIQFGGA EVSGFQIVDY DDSLVSKFIE RWSTLEEKEY PGAHTATIKY TSALTYDAVQ VMTEAFRNLR KQRIEISRRG NAGDCLANPA VPWGQGVEIE RALKQVQVEG LSGNIKFDQN GKRINYTINI MELKTNGPRK IGYWSEVDKM VLTEDDTSGL EQKTVVVTTI LESPYVMMKA NHAALAGNER YEGYCVDLAA EIAKHCGFKY KLTIVGDGKY GARDADTKIW NGMVGELVYG KADIAIAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHTEEFEDGR ETQSSESTNE FGIFNSLWFS LGAFMQQGAD ISPRSLSGRI VGGVWWFFTL IIISSYTANL AAFLTVERMV SPIESAEDLS KQTEIAYGTL DSGSTKEFFR RSKIAVFDKM WTYMRSAEPS VFVRTTAEGV ARVRKSKGKY AYLLESTMNE YIEQRKPCDT MKVGGNLDSK GYGIATPKGS SLGTPVNLAV LKLSEQGLLD KLKNKWWYDK GECGAKDSGS KEKTSALSLS NVAGVFYILV GGLGLAMLVA LIEFCYKSRA EAKRMKGLVP RG

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Experimental information

BeamInstrument name: FRM2 KWS1 / City: Munich / 国: Germany / Type of source: neutron source / Wavelength: 0.5 Å
DetectorName: ?? / Type: 6Li-Scintillator 1 mm thickness + photomultiplier / Pixsize x: 5.3 mm
Scan
Title: Glutamate receptor 2 (GluA2) in the resting state / Measurement date: Sep 19, 2017 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 900 sec. / Number of frames: 15 / Unit: 1/A /
MinMax
Q0.006 0.2127
ResultType of curve: single_conc
Comments: Sample of GluA2 in the resting state (apo). The SANS data were fitted with a mixture of GluA2 in the tetrameric resting state (pdb-code 4u2p) and a fraction of oligomers of the tetramer ...Comments: Sample of GluA2 in the resting state (apo). The SANS data were fitted with a mixture of GluA2 in the tetrameric resting state (pdb-code 4u2p) and a fraction of oligomers of the tetramer (best fit: fit54.dat). The oligomers were described with a fractal structure factor (Teixeira, J. (1988). J. Appl. Crystallogr. 21, 781-785). Data were fitted with WillItFit (Pedersen, M. C., Arleth, L. & Mortensen, K. (2013). J. Appl. Crystallogr. 46, 1894-1898). The SANS data were measured in three settings (sample/collimation): 1.5m/4m, 4m/4m, and 8m/8m. The attached data are merged into one data set with all three settings. Pair distance distribution functions were calculated with BayesApp (www.bayesapp.org). Due to relatively low protein concentration, the concentration measurement was inaccurate, and the MW was therefore evaluated by (concentration independent) Porod analysis using the Porod volume calculator implemented in PRIMUS, and with a volume-to-mass conversion constant of 0.83 kDa/nm^3 (Gekko, K. & Noguchi, H. (1979). J. Phys. Chem. 83, 2706-2714; Squire, P. G. & Himmel, M. E. (1979). Arch. Biochem. Biophys. 196, 165-177).
ExperimentalPorod
MW329 kDa329 kDa
Volume-396 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.0444 0.000185 0.043 0.00085
Radius of gyration, Rg6.19 nm0.04 5.96 nm0.29

MinMaxError
D-17.9 6.2
Guinier point1 22 -

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