1nnk

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[[Image:1nnk.gif|left|200px]]
 
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{{Structure
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==X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.85 A resolution. Crystallization with zinc ions.==
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|PDB= 1nnk |SIZE=350|CAPTION= <scene name='initialview01'>1nnk</scene>, resolution 1.85&Aring;
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<StructureSection load='1nnk' size='340' side='right'caption='[[1nnk]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CE2:3-(5-TERT-BUTYL-3-OXIDOISOXAZOL-4-YL)-L-ALANINATE'>CE2</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1nnk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NNK FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CE2:3-(5-TERT-BUTYL-3-OXIDOISOXAZOL-4-YL)-L-ALANINATE'>CE2</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nnk OCA], [https://pdbe.org/1nnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nnk RCSB], [https://www.ebi.ac.uk/pdbsum/1nnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nnk ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ftj|1FTJ]], [[1ftk|1FTK]], [[1fto|1FTO]], [[1fw0|1FW0]], [[1ftl|1FTL]], [[1gr2|1GR2]], [[1lb8|1LB8]], [[1lb9|1LB9]], [[1lbc|1LBC]], [[1m5e|1M5E]], [[1m5c|1M5C]], [[1m5b|1M5B]], [[1m5f|1M5F]], [[1mm7|1MM7]], [[1mm6|1MM6]], [[1lbb|1LBB]], [[1my4|1MY4]], [[1my3|1MY3]], [[1m5d|1M5D]], [[1ftm|1FTM]], [[1nnp|1NNP]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nnk OCA], [http://www.ebi.ac.uk/pdbsum/1nnk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nnk RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/GRIA2_RAT GRIA2_RAT] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.<ref>PMID:9351977</ref> <ref>PMID:19265014</ref> <ref>PMID:21172611</ref> <ref>PMID:12501192</ref> <ref>PMID:12015593</ref> <ref>PMID:12872125</ref> <ref>PMID:12730367</ref> <ref>PMID:16192394</ref> <ref>PMID:15591246</ref> <ref>PMID:17018279</ref> <ref>PMID:16483599</ref> <ref>PMID:19946266</ref> <ref>PMID:21317873</ref> <ref>PMID:21846932</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/1nnk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nnk ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Two X-ray structures of the GluR2 ligand-binding core in complex with (S)-2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionic acid ((S)-ATPA) have been determined with and without Zn(2+) ions. (S)-ATPA induces a domain closure of ca. 21 degrees compared to the apo form. The tert-butyl moiety of (S)-ATPA is buried in a partially hydrophobic pocket and forces the ligand into the glutamate-like binding mode. The structures provide new insight into the molecular basis of agonist selectivity between AMPA and kainate receptors.
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'''X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.85 A resolution. Crystallization with zinc ions.'''
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Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity.,Lunn ML, Hogner A, Stensbol TB, Gouaux E, Egebjerg J, Kastrup JS J Med Chem. 2003 Feb 27;46(5):872-5. PMID:12593667<ref>PMID:12593667</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1nnk" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Two X-ray structures of the GluR2 ligand-binding core in complex with (S)-2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionic acid ((S)-ATPA) have been determined with and without Zn(2+) ions. (S)-ATPA induces a domain closure of ca. 21 degrees compared to the apo form. The tert-butyl moiety of (S)-ATPA is buried in a partially hydrophobic pocket and forces the ligand into the glutamate-like binding mode. The structures provide new insight into the molecular basis of agonist selectivity between AMPA and kainate receptors.
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1NNK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NNK OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity., Lunn ML, Hogner A, Stensbol TB, Gouaux E, Egebjerg J, Kastrup JS, J Med Chem. 2003 Feb 27;46(5):872-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12593667 12593667]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Egebjerg J]]
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[[Category: Egebjerg, J.]]
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[[Category: Gouaux E]]
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[[Category: Gouaux, E.]]
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[[Category: Hogner A]]
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[[Category: Hogner, A.]]
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[[Category: Kastrup JS]]
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[[Category: Kastrup, J S.]]
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[[Category: Lunn M-L]]
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[[Category: Lunn, M L.]]
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[[Category: Stensbol TB]]
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[[Category: Stensbol, T B.]]
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[[Category: agonist complex]]
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[[Category: ionotropic glutamate receptor glur2]]
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[[Category: ligand-binding core]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:32:51 2008''
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Current revision

X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.85 A resolution. Crystallization with zinc ions.

PDB ID 1nnk

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