2wjx: Difference between revisions
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==Crystal structure of the human ionotropic glutamate receptor GluR2 ATD region at 4.1 A resolution== | |||
<StructureSection load='2wjx' size='340' side='right'caption='[[2wjx]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2wjx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WJX FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wjw|2wjw]]</div></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=2wjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wjx OCA], [https://pdbe.org/2wjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wjx RCSB], [https://www.ebi.ac.uk/pdbsum/2wjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wjx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/GRIA2_HUMAN GRIA2_HUMAN]] 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:20614889</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wj/2wjx_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2wjx ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-A resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-A resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic data for full-length AMPA receptors. | |||
Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.,Clayton A, Siebold C, Gilbert RJ, Sutton GC, Harlos K, McIlhinney RA, Jones EY, Aricescu AR J Mol Biol. 2009 Oct 9;392(5):1125-32. Epub 2009 Aug 3. PMID:19651138<ref>PMID:19651138</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2wjx" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[ | *[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Aricescu, A R | [[Category: Human]] | ||
[[Category: Clayton, A | [[Category: Large Structures]] | ||
[[Category: Gilbert, R J.C | [[Category: Aricescu, A R]] | ||
[[Category: Harlos, K | [[Category: Clayton, A]] | ||
[[Category: Jones, E Y | [[Category: Gilbert, R J.C]] | ||
[[Category: | [[Category: Harlos, K]] | ||
[[Category: Siebold, C | [[Category: Jones, E Y]] | ||
[[Category: Sutton, G C | [[Category: McIlhinney, R A.J]] | ||
[[Category: Siebold, C]] | |||
[[Category: Sutton, G C]] | |||
[[Category: Alternative splicing]] | |||
[[Category: Cell junction]] | [[Category: Cell junction]] | ||
[[Category: Cell membrane]] | [[Category: Cell membrane]] | ||
| Line 36: | Line 58: | ||
[[Category: Palmitate]] | [[Category: Palmitate]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Polymorphism]] | |||
[[Category: Postsynaptic cell membrane]] | [[Category: Postsynaptic cell membrane]] | ||
[[Category: Receptor]] | [[Category: Receptor]] | ||
