4pas - Revision history

OCA at 00:42, 28 December 2023

2023-12-28T00:42:09Z

← Older revision		Revision as of 00:42, 28 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PAS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
	</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [https://pdbe.org/4pas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [https://www.ebi.ac.uk/pdbsum/4pas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas ProSAT]</span></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]] 1.62Å</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [https://pdbe.org/4pas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [https://www.ebi.ac.uk/pdbsum/4pas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 12:50, 1 February 2023

2023-02-01T12:50:02Z

← Older revision		Revision as of 12:50, 1 February 2023
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	<StructureSection load='4pas' size='340' side='right'caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>		<StructureSection load='4pas' size='340' side='right'caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4PAS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GABBR1, GPRC3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GABBR2, GPR51, GPRC3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [https://pdbe.org/4pas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [https://www.ebi.ac.uk/pdbsum/4pas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas 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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [~~http~~://pdbe.org/4pas PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4pas PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/GABR1_HUMAN GABR1_HUMAN]] Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Activated by (-)-baclofen, cgp27492 and blocked by phaclofen.<ref>PMID:9844003</ref> <ref>PMID:9872316</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref> Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites.<ref>PMID:9844003</ref> <ref>PMID:9872316</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref> [[http://www.uniprot.org/uniprot/GABR2_HUMAN GABR2_HUMAN]] Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.<ref>PMID:9872316</ref> <ref>PMID:10328880</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref>		[https://www.uniprot.org/uniprot/GABR1_HUMAN GABR1_HUMAN] Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Activated by (-)-baclofen, cgp27492 and blocked by phaclofen.<ref>PMID:9844003</ref> <ref>PMID:9872316</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref> Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites.<ref>PMID:9844003</ref> <ref>PMID:9872316</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Burmakina, S]]		[[Category: Burmakina S]]
	[[Category: Chen, Y]]		[[Category: Chen Y]]
	[[Category: Fan~~, Q R~~]]		[[Category: Fan QR]]
	[[Category: Geng, Y]]		[[Category: Geng Y]]
	~~[[Category: Coiled-coil]]~~
	~~[[Category: Heterodimer]]~~
	~~[[Category: Signaling protein~~]]

OCA at 10:10, 25 December 2019

2019-12-25T10:10:46Z

← Older revision		Revision as of 10:10, 25 December 2019
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	==Heterodimeric coiled-coil structure of human GABA(B) receptor==		==Heterodimeric coiled-coil structure of human GABA(B) receptor==
	<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>		<StructureSection load='4pas' size='340' side='right'caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4pas" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4pas" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[GABA receptor 3D structures\|GABA receptor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Burmakina, S]]		[[Category: Burmakina, S]]
	[[Category: Chen, Y]]		[[Category: Chen, Y]]

OCA at 11:58, 6 November 2017

2017-11-06T11:58:26Z

← Older revision		Revision as of 11:58, 6 November 2017
Line 3:		Line 3:
	<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>		<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
	</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://pdbe.org/4pas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas ProSAT]</span></td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GABBR1, GPRC3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), GABBR2, GPR51, GPRC3B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://pdbe.org/4pas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 4pas" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4pas" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[GABA receptor\|GABA receptor]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Human]]
	[[Category: Burmakina, S]]		[[Category: Burmakina, S]]
	[[Category: Chen, Y]]		[[Category: Chen, Y]]

OCA at 17:33, 4 August 2016

2016-08-04T17:33:11Z

← Older revision		Revision as of 17:33, 4 August 2016
Line 1:		Line 1:

	==Heterodimeric coiled-coil structure of human GABA(B) receptor==		==Heterodimeric coiled-coil structure of human GABA(B) receptor==
	<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>		<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
	</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>		</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://pdbe.org/4pas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pas ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 4pas" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[GABA receptor\|GABA receptor]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:26, 25 December 2014

2014-12-25T11:26:55Z

← Older revision		Revision as of 11:26, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>		</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=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/GABR1_HUMAN GABR1_HUMAN]] Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Activated by (-)-baclofen, cgp27492 and blocked by phaclofen.<ref>PMID:9844003</ref> <ref>PMID:9872316</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref> Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites.<ref>PMID:9844003</ref> <ref>PMID:9872316</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref> [[http://www.uniprot.org/uniprot/GABR2_HUMAN GABR2_HUMAN]] Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.<ref>PMID:9872316</ref> <ref>PMID:10328880</ref> <ref>PMID:18165688</ref> <ref>PMID:22660477</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Burmakina, S.]]		[[Category: Burmakina, S]]
	[[Category: Chen, Y.]]		[[Category: Chen, Y]]
	[[Category: Fan, Q R.]]		[[Category: Fan, Q R]]
	[[Category: Geng, Y.]]		[[Category: Geng, Y]]
	[[Category: Coiled-coil]]		[[Category: Coiled-coil]]
	[[Category: Heterodimer]]		[[Category: Heterodimer]]
	[[Category: Signaling protein]]		[[Category: Signaling protein]]

OCA at 06:35, 11 June 2014

2014-06-11T06:35:19Z

← Older revision		Revision as of 06:35, 11 June 2014
Line 2:		Line 2:
	<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>		<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. ~~<br>~~		<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PAS FirstGlance]. <br>
	~~</td></tr><tr><td class="sblockLbl">~~<b>~~Activity:~~</b>~~</td><td class="sblockDat"><span class='plainlinks'>~~[http://en.~~wikipedia~~.~~org/wiki/Glucokinase Glucokinase], with EC number [http:/~~/~~www.brenda~~-~~enzymes.info~~/~~php~~/~~result_flat~~.~~php4~~?~~ecno~~=2.~~7.1.2 2.7.1.2]~~ <~~/span~~></td></tr>		</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>
	<table>		<table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 12:		Line 11:
	Heterodimeric coiled-coil interactions of human GABAB receptor.,Burmakina S, Geng Y, Chen Y, Fan QR Proc Natl Acad Sci U S A. 2014 Apr 28. PMID:24778228<ref>PMID:24778228</ref>		Heterodimeric coiled-coil interactions of human GABAB receptor.,Burmakina S, Geng Y, Chen Y, Fan QR Proc Natl Acad Sci U S A. 2014 Apr 28. PMID:24778228<ref>PMID:24778228</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==

OCA at 06:52, 14 May 2014

2014-05-14T06:52:11Z

← Older revision		Revision as of 06:52, 14 May 2014
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	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>
	<table>		<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Metabotropic GABAB receptor is a G protein-coupled receptor that mediates inhibitory neurotransmission in the CNS. It functions as an obligatory heterodimer of GABAB receptor 1 (GBR1) and GABAB receptor 2 (GBR2) subunits. The association between GBR1 and GBR2 masks an endoplasmic reticulum (ER) retention signal in the cytoplasmic region of GBR1 and facilitates cell surface expression of both subunits. Here, we present, to our knowledge, the first crystal structure of an intracellular coiled-coil heterodimer of human GABAB receptor. We found that polar interactions buried within the hydrophobic core determine the specificity of heterodimer pairing. Disruption of the hydrophobic coiled-coil interface with single mutations in either subunit impairs surface expression of GBR1, confirming that the coiled-coil interaction is required to inactivate the adjacent ER retention signal of GBR1. The coiled-coil assembly buries an internalization motif of GBR1 at the heterodimer interface. The ER retention signal of GBR1 is not part of the core coiled-coil structure, suggesting that it is sterically shielded by GBR2 upon heterodimer formation.

			Heterodimeric coiled-coil interactions of human GABAB receptor.,Burmakina S, Geng Y, Chen Y, Fan QR Proc Natl Acad Sci U S A. 2014 Apr 28. PMID:24778228<ref>PMID:24778228</ref>

			From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
			</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:23, 7 May 2014

2014-05-07T08:23:44Z

← Older revision		Revision as of 08:23, 7 May 2014
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	'''~~Unreleased structure~~'''		==Heterodimeric coiled-coil structure of human GABA(B) receptor==
			<StructureSection load='4pas' size='340' side='right' caption='[[4pas]], [[Resolution\|resolution]] 1.62Å' scene=''>
	~~The entry~~ 4pas is ~~ON HOLD until Paper Publication~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4pas]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAS OCA]. <br>
	~~Authors~~: ~~Burmakina~~, S., ~~Geng~~, Y., Chen, Y., Fan, Q.R.		</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pas RCSB], [http://www.ebi.ac.uk/pdbsum/4pas PDBsum]</span></td></tr>
	~~Description~~: ~~Heterodimeric coiled~~-coil ~~structure of human GABA(B) receptor~~		<table>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Burmakina, S.]]
			[[Category: Chen, Y.]]
			[[Category: Fan, Q R.]]
			[[Category: Geng, Y.]]
			[[Category: Coiled-coil]]
			[[Category: Heterodimer]]
			[[Category: Signaling protein]]

OCA at 07:23, 23 April 2014

2014-04-23T07:23:51Z

← Older revision		Revision as of 07:23, 23 April 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4pas is ON HOLD		The entry 4pas is ON HOLD until Paper Publication

	Authors: Burmakina, S., Geng, Y., Chen, Y., Fan, Q.R.		Authors: Burmakina, S., Geng, Y., Chen, Y., Fan, Q.R.

	Description: Heterodimeric coiled-coil structure of human GABA(B) receptor		Description: Heterodimeric coiled-coil structure of human GABA(B) receptor