4gxs - Revision history

OCA at 15:59, 14 March 2024

2024-03-14T15:59:09Z

←Older revision		Revision as of 15:59, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gxs]] is a 2 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=4GXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gxs]] is a 2 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=4GXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.9634Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [https://pdbe.org/4gxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [https://www.ebi.ac.uk/pdbsum/4gxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxs ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [https://pdbe.org/4gxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [https://www.ebi.ac.uk/pdbsum/4gxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[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>		[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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Glutamate receptors mediate the majority of excitatory synaptic transmission in the central nervous system and excessive stimulation of these receptors is involved in a variety of neurological disorders and neuronal damage from stroke. The development of new subtype specific antagonists would be of considerable therapeutic interest. Natural products can provide important new lead compounds for drug discovery. The only natural product known to inhibit glutamate receptors competitively is (-)-kaitocephalin, which was isolated from the fungus, Eupenicillium shearii and found to protect CNS neurons from excitotoxicity. Previous work has shown that it is a potent antagonist of some subtypes of glutamate receptors (AMPA and NMDA, but not kainate). The structure of kaitocephalin bound to the ligand-binding domain of the AMPA receptor subtype, GluA2, is reported here. The structure suggests how kaitocephalin can be used as a scaffold to develop more selective and high affinity antagonists for glutamate receptors.
-
-	The Structure of (-)-Kaitocephalin Bound to the Ligand Binding Domain of the AMPA/Glutamate Receptor, GluA2.,Ahmed AH, Hamada M, Shinada T, Ohfune Y, Weerasinghe L, Garner PP, Oswald RE J Biol Chem. 2012 Oct 17. PMID:23076153<ref>PMID:23076153</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gxs" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 07:24, 26 October 2022

2022-10-26T07:24:59Z

←Older revision		Revision as of 07:24, 26 October 2022
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	==Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin==		==Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin==
-	<StructureSection load='4gxs' size='340' side='right' caption='[[4gxs]], [[Resolution\|resolution]] 1.96Å' scene=''>	+	<StructureSection load='4gxs' size='340' side='right'caption='[[4gxs]], [[Resolution\|resolution]] 1.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gxs]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GXS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gxs]] is a 2 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=4GXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXS FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Glur2, Gria2, Gria2; GluA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [https://pdbe.org/4gxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [https://www.ebi.ac.uk/pdbsum/4gxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxs ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [~~http~~://pdbe.org/4gxs PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gxs PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxs ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4gxs" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4gxs" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutamate receptor 3D structures\|Glutamate receptor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Ahmed, A H~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Oswald, R E~~]]	+	[[Category: Ahmed AH]]
-	[[Category: ~~Ampa receptor]]~~	+	[[Category: Oswald RE]]
-	~~[[Category: Glua2]]~~	+
-	~~[[Category: Glur2]]~~	+
-	~~[[Category: Glutamate receptor]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Neurotransmitter receptor~~]]	+

OCA at 02:45, 16 November 2017

2017-11-16T02:45:07Z

←Older revision		Revision as of 02:45, 16 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4gxs" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4gxs" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Ionotropic Glutamate Receptors\|Ionotropic Glutamate Receptors]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:11, 5 August 2016

2016-08-05T21:11:44Z

←Older revision		Revision as of 21:11, 5 August 2016
Line 1:		Line 1:
		+
	==Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin==		==Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin==
	<StructureSection load='4gxs' size='340' side='right' caption='[[4gxs]], [[Resolution\|resolution]] 1.96Å' scene=''>		<StructureSection load='4gxs' size='340' side='right' caption='[[4gxs]], [[Resolution\|resolution]] 1.96Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gxs]] is a 2 chain structure with 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=4GXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXS FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gxs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXS FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Glur2, Gria2, Gria2; GluA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Glur2, Gria2, Gria2; GluA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [http://www.ebi.ac.uk/pdbsum/4gxs PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [http://pdbe.org/4gxs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [http://www.ebi.ac.uk/pdbsum/4gxs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxs ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gxs" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Ahmed, A H]]		[[Category: Ahmed, A H]]
	[[Category: Oswald, R E]]		[[Category: Oswald, R E]]

OCA at 05:55, 25 December 2014

2014-12-25T05:55:10Z

←Older revision		Revision as of 05:55, 25 December 2014
Line 7:		Line 7:
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [http://www.ebi.ac.uk/pdbsum/4gxs PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [http://www.ebi.ac.uk/pdbsum/4gxs PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:52, 21 December 2014

2014-12-21T10:52:05Z

←Older revision		Revision as of 10:52, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4gxs\| PDB=4gxs \| SCENE= }}~~	+	==Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin==
-	===Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin===	+	<StructureSection load='4gxs' size='340' side='right' caption='[[4gxs]], [[Resolution\|resolution]] 1.96Å' scene=''>
-	{~~{ABSTRACT_PUBMED_23076153}~~}	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gxs]] is a 2 chain structure with 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=4GXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXS FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0YS:(5R)-2-[(1S,2R)-2-AMINO-2-CARBOXY-1-HYDROXYETHYL]-5-{(2S)-2-CARBOXY-2-[(3,5-DICHLORO-4-HYDROXYBENZOYL)AMINO]ETHYL}-L-PROLINE'>0YS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Glur2, Gria2, Gria2; GluA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxs RCSB], [http://www.ebi.ac.uk/pdbsum/4gxs PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glutamate receptors mediate the majority of excitatory synaptic transmission in the central nervous system and excessive stimulation of these receptors is involved in a variety of neurological disorders and neuronal damage from stroke. The development of new subtype specific antagonists would be of considerable therapeutic interest. Natural products can provide important new lead compounds for drug discovery. The only natural product known to inhibit glutamate receptors competitively is (-)-kaitocephalin, which was isolated from the fungus, Eupenicillium shearii and found to protect CNS neurons from excitotoxicity. Previous work has shown that it is a potent antagonist of some subtypes of glutamate receptors (AMPA and NMDA, but not kainate). The structure of kaitocephalin bound to the ligand-binding domain of the AMPA receptor subtype, GluA2, is reported here. The structure suggests how kaitocephalin can be used as a scaffold to develop more selective and high affinity antagonists for glutamate receptors.

-	~~==Function==~~	+	The Structure of (-)-Kaitocephalin Bound to the Ligand Binding Domain of the AMPA/Glutamate Receptor, GluA2.,Ahmed AH, Hamada M, Shinada T, Ohfune Y, Weerasinghe L, Garner PP, Oswald RE J Biol Chem. 2012 Oct 17. PMID:23076153<ref>PMID:23076153</ref>
-	~~[[http://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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4gxs]] is~~ a ~~2 chain structure with 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=4GXS OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023076153</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Ionotropic Glutamate Receptors\|Ionotropic Glutamate Receptors]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Ahmed, A H.]]	+	[[Category: Ahmed, A H]]
-	[[Category: Oswald, R E.]]	+	[[Category: Oswald, R E]]
	[[Category: Ampa receptor]]		[[Category: Ampa receptor]]
	[[Category: Glua2]]		[[Category: Glua2]]

OCA at 07:45, 20 June 2013

2013-06-20T07:45:42Z

←Older revision		Revision as of 07:45, 20 June 2013
Line 1:		Line 1:
-	[[Image:4gxs.png\|left\|200px]]
-
	{{STRUCTURE_4gxs\| PDB=4gxs \| SCENE= }}		{{STRUCTURE_4gxs\| PDB=4gxs \| SCENE= }}
-
	===Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin===		===Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin===
		+	{{ABSTRACT_PUBMED_23076153}}

		+	==Function==
		+	[[http://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>

	==About this Structure==		==About this Structure==
	[[4gxs]] is a 2 chain structure with 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=4GXS OCA].		[[4gxs]] is a 2 chain structure with 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=4GXS OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023076153</ref><references group="xtra"/><references/>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Ahmed, A H.]]		[[Category: Ahmed, A H.]]

OCA at 13:51, 8 November 2012

2012-11-08T13:51:16Z

←Older revision		Revision as of 13:51, 8 November 2012
Line 1:		Line 1:
-	[[Image:4gxs.~~jpg~~\|left\|200px]]	+	[[Image:4gxs.png\|left\|200px]]

	{{STRUCTURE_4gxs\| PDB=4gxs \| SCENE= }}		{{STRUCTURE_4gxs\| PDB=4gxs \| SCENE= }}

OCA at 07:14, 17 October 2012

2012-10-17T07:14:54Z

←Older revision		Revision as of 07:14, 17 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gxs.jpg\|left\|200px]]

-	~~The entry~~ 4gxs ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gxs\| PDB=4gxs \| SCENE= }}

-	~~Authors: Ahmed, A.H., Oswald, R.E.~~	+	===Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin===

-	~~Description~~: ~~Ligand binding domain of GluA2 (AMPA~~/~~glutamate receptor) bound to (~~-~~)-kaitocephalin~~	+
		+	==About this Structure==
		+	[[4gxs]] is a 2 chain structure with 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=4GXS OCA].
		+	[[Category: Rattus norvegicus]]
		+	[[Category: Ahmed, A H.]]
		+	[[Category: Oswald, R E.]]
		+	[[Category: Ampa receptor]]
		+	[[Category: Glua2]]
		+	[[Category: Glur2]]
		+	[[Category: Glutamate receptor]]
		+	[[Category: Membrane protein]]
		+	[[Category: Neurotransmitter receptor]]

OCA at 06:54, 10 October 2012

2012-10-10T06:54:20Z

←Older revision		Revision as of 06:54, 10 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gxs is ON HOLD	+	The entry 4gxs is ON HOLD until Paper Publication

	Authors: Ahmed, A.H., Oswald, R.E.		Authors: Ahmed, A.H., Oswald, R.E.

	Description: Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin		Description: Ligand binding domain of GluA2 (AMPA/glutamate receptor) bound to (-)-kaitocephalin