3n6v

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[[Image:3n6v.png|left|200px]]
 
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{{STRUCTURE_3n6v| PDB=3n6v | SCENE= }}
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==Structure of the GluA2 NTD-dimer interface mutant, T78A==
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<StructureSection load='3n6v' size='340' side='right'caption='[[3n6v]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3n6v]] is a 6 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=3N6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N6V FirstGlance]. <br>
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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]] 3.2&#8491;</td></tr>
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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=3n6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n6v OCA], [https://pdbe.org/3n6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n6v RCSB], [https://www.ebi.ac.uk/pdbsum/3n6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n6v ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The assembly of AMPA-type glutamate receptors (AMPARs) into distinct ion channel tetramers ultimately governs the nature of information transfer at excitatory synapses. How cells regulate the formation of diverse homo- and heteromeric AMPARs is unknown. Using a sensitive biophysical approach, we show that the extracellular, membrane-distal AMPAR N-terminal domains (NTDs) orchestrate selective routes of heteromeric assembly via a surprisingly wide spectrum of subunit-specific association affinities. Heteromerization is dominant, occurs at the level of the dimer, and results in a preferential incorporation of the functionally critical GluA2 subunit. Using a combination of structure-guided mutagenesis and electrophysiology, we further map evolutionarily variable hotspots in the NTD dimer interface, which modulate heteromerization capacity. This 'flexibility' of the NTD not only explains why heteromers predominate but also how GluA2-lacking, Ca(2+)-permeable homomers could form, which are induced under specific physiological and pathological conditions. Our findings reveal that distinct NTD properties set the stage for the biogenesis of functionally diverse pools of homo- and heteromeric AMPAR tetramers.
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===Structure of the GluA2 NTD-dimer interface mutant, T78A===
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Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers.,Rossmann M, Sukumaran M, Penn AC, Veprintsev DB, Babu MM, Greger IH EMBO J. 2011 Mar 2;30(5):959-71. Epub 2011 Feb 11. PMID:21317873<ref>PMID:21317873</ref>
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{{ABSTRACT_PUBMED_21317873}}
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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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==About this Structure==
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<div class="pdbe-citations 3n6v" style="background-color:#fffaf0;"></div>
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[[3n6v]] is a 6 chain structure of [[Ionotropic Glutamate Receptors]] 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=3N6V OCA].
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==See Also==
==See Also==
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*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021317873</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Greger, I H.]]
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[[Category: Greger IH]]
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[[Category: Rossmann, M.]]
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[[Category: Rossmann M]]
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[[Category: Sukumaran, M.]]
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[[Category: Sukumaran M]]
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[[Category: Ampa]]
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[[Category: Assembly]]
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[[Category: Glua2]]
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[[Category: Glur2]]
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[[Category: Ntd]]
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[[Category: Transport protein]]
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Current revision

Structure of the GluA2 NTD-dimer interface mutant, T78A

PDB ID 3n6v

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