9qdn: Difference between revisions

Latest revision as of 05:48, 24 September 2025

GluA4 in complex with TARP-2, resting state I, structure of TMD/LBD

Structural highlights

9qdn is a 8 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.71Å
Ligands:	E2Q, OLC, PLM
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCG2_RAT Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Milstein AD, Zhou W, Karimzadegan S, Bredt DS, Nicoll RA. TARP subtypes differentially and dose-dependently control synaptic AMPA receptor gating. Neuron. 2007 Sep 20;55(6):905-18. PMID:17880894 doi:https://dx.doi.org/10.1016/j.neuron.2007.08.022
↑ Kato AS, Siuda ER, Nisenbaum ES, Bredt DS. AMPA receptor subunit-specific regulation by a distinct family of type II TARPs. Neuron. 2008 Sep 25;59(6):986-96. doi: 10.1016/j.neuron.2008.07.034. PMID:18817736 doi:https://dx.doi.org/10.1016/j.neuron.2008.07.034
↑ Soto D, Coombs ID, Renzi M, Zonouzi M, Farrant M, Cull-Candy SG. Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5. Nat Neurosci. 2009 Mar;12(3):277-85. doi: 10.1038/nn.2266. Epub 2009 Feb 22. PMID:19234459 doi:https://dx.doi.org/10.1038/nn.2266
↑ Schwenk J, Harmel N, Zolles G, Bildl W, Kulik A, Heimrich B, Chisaka O, Jonas P, Schulte U, Fakler B, Klocker N. Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors. Science. 2009 Mar 6;323(5919):1313-9. doi: 10.1126/science.1167852. PMID:19265014 doi:10.1126/science.1167852
↑ Shi Y, Suh YH, Milstein AD, Isozaki K, Schmid SM, Roche KW, Nicoll RA. Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating. Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16315-9. doi:, 10.1073/pnas.1011706107. Epub 2010 Aug 30. PMID:20805473 doi:https://dx.doi.org/10.1073/pnas.1011706107

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OCA

[1] Milstein AD, Zhou W, Karimzadegan S, Bredt DS, Nicoll RA. TARP subtypes differentially and dose-dependently control synaptic AMPA receptor gating. Neuron. 2007 Sep 20;55(6):905-18. PMID:17880894 doi:https://dx.doi.org/10.1016/j.neuron.2007.08.022

[2] Kato AS, Siuda ER, Nisenbaum ES, Bredt DS. AMPA receptor subunit-specific regulation by a distinct family of type II TARPs. Neuron. 2008 Sep 25;59(6):986-96. doi: 10.1016/j.neuron.2008.07.034. PMID:18817736 doi:https://dx.doi.org/10.1016/j.neuron.2008.07.034

[3] Soto D, Coombs ID, Renzi M, Zonouzi M, Farrant M, Cull-Candy SG. Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5. Nat Neurosci. 2009 Mar;12(3):277-85. doi: 10.1038/nn.2266. Epub 2009 Feb 22. PMID:19234459 doi:https://dx.doi.org/10.1038/nn.2266

[4] Schwenk J, Harmel N, Zolles G, Bildl W, Kulik A, Heimrich B, Chisaka O, Jonas P, Schulte U, Fakler B, Klocker N. Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors. Science. 2009 Mar 6;323(5919):1313-9. doi: 10.1126/science.1167852. PMID:19265014 doi:10.1126/science.1167852

[5] Shi Y, Suh YH, Milstein AD, Isozaki K, Schmid SM, Roche KW, Nicoll RA. Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating. Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16315-9. doi:, 10.1073/pnas.1011706107. Epub 2010 Aug 30. PMID:20805473 doi:https://dx.doi.org/10.1073/pnas.1011706107

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9qdn is ON HOLD  until Paper Publication
+==GluA4 in complex with TARP-2, resting state I, structure of TMD/LBD==
+<StructureSection load='9qdn' size='340' side='right'caption='[[9qdn]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9qdn]] is a 8 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=9QDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QDN FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E2Q:6-nitro-2,3-bis(oxidanylidene)-1,4-dihydrobenzo[f]quinoxaline-7-sulfonamide'>E2Q</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=9qdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qdn OCA], [https://pdbe.org/9qdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qdn RCSB], [https://www.ebi.ac.uk/pdbsum/9qdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qdn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CCG2_RAT CCG2_RAT] Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.<ref>PMID:17880894</ref> <ref>PMID:18817736</ref> <ref>PMID:19234459</ref> <ref>PMID:19265014</ref> <ref>PMID:20805473</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Rattus norvegicus]]
+[[Category: Herguedas B]]
+[[Category: Vega-Gutierrez C]]

9qdn: Difference between revisions

Latest revision as of 05:48, 24 September 2025

GluA4 in complex with TARP-2, resting state I, structure of TMD/LBD

Structural highlights

Function

References

Contents

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