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

Basic information

Entry

Database: SASBDB / ID: SASDDY5

Sample

AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents

• Glutamate receptor 2 (protein), GluA2, Rattus norvegicus

Function / homology

Function:

spine synapse / dendritic spine neck / dendritic spine head / Activation of AMPA receptors / perisynaptic space / AMPA glutamate receptor activity / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / immunoglobulin binding / AMPA glutamate receptor complex / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / extracellularly glutamate-gated ion channel activity / cellular response to glycine / asymmetric synapse / regulation of receptor recycling / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of synaptic transmission / glutamate receptor binding / extracellular ligand-gated monoatomic ion channel activity / glutamate-gated receptor activity / response to fungicide / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / regulation of synaptic transmission, glutamatergic / somatodendritic compartment / dendrite membrane / cellular response to brain-derived neurotrophic factor stimulus / cytoskeletal protein binding / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / ionotropic glutamate receptor binding / dendrite cytoplasm / ionotropic glutamate receptor signaling pathway / SNARE binding / dendritic shaft / synaptic transmission, glutamatergic / synaptic membrane / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / PDZ domain binding / protein tetramerization / postsynaptic density membrane / establishment of protein localization / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / terminal bouton / receptor internalization / cerebral cortex development / synaptic vesicle membrane / synaptic vesicle / presynapse / signaling receptor activity / presynaptic membrane / amyloid-beta binding / growth cone / scaffold protein binding / chemical synaptic transmission / perikaryon / postsynaptic membrane / dendritic spine / postsynaptic density / neuron projection / axon / neuronal cell body / glutamatergic synapse / dendrite / synapse / protein-containing complex binding / protein kinase binding / cell surface / endoplasmic reticulum / protein-containing complex / identical protein binding / membrane / plasma membrane

Domain/homology:

Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : / 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

Component:

Glutamate receptor 2

• Biological species: Rattus norvegicus (Norway rat)

Contact author

• Andreas Larsen (University of Copenhagen, Copenhagen, Denmark)

Models

Sample

• Sample: Name: AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents; Specimen concentration: 0.34 mg/ml
• Buffer: Name: 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 #1037

Name: GluA2 / Type: protein / Description: Glutamate receptor 2 / 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 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

Experimental information

• Beam: Instrument name: FRM2 KWS1 / City: Munich / 国: Germany / Type of source: neutron source / Wavelength: 0.5 Å
• Detector: Name: ?? / 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 /

	Min	Max
Q	0.006	0.2127

Result

Type 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 (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).

	Experimental	Porod
MW	329 kDa	329 kDa
Volume	-	396 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.0444	0.000185	0.043	0.00085
Radius of gyration, Rg	6.19 nm	0.04	5.96 nm	0.29

	Min	Max	Error
D	-	17.9	6.2
Guinier point	1	22	-