3en3

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{{Seed}}
 
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[[Image:3en3.jpg|left|200px]]
 
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==Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate==
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The line below this paragraph, containing "STRUCTURE_3en3", creates the "Structure Box" on the page.
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<StructureSection load='3en3' size='340' side='right'caption='[[3en3]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3en3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EN3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KAI:3-(CARBOXYMETHYL)-4-ISOPROPENYLPROLINE'>KAI</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3epe|3epe]]</div></td></tr>
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{{STRUCTURE_3en3| PDB=3en3 | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Glur4,Glutamate receptor ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=3en3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3en3 OCA], [https://pdbe.org/3en3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3en3 RCSB], [https://www.ebi.ac.uk/pdbsum/3en3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3en3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/GRIA4_RAT GRIA4_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 (By similarity).<ref>PMID:12603841</ref> <ref>PMID:19102704</ref> <ref>PMID:20107073</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/en/3en3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3en3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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AMPA receptors are glutamate-gated ion channels that are essential mediators of synaptic signals in the central nervous system. They form tetramers that are assembled as combinations of subunits GluR1-4, each of which contains a ligand-binding domain (LBD). Crystal structures of the GluR2 LBD have revealed an agonist-binding cleft, which is located between two lobes and which acts like a Venus flytrap. In general, agonist efficacy is correlated with the extent of cleft closure. However, recent observations show that cleft closure is not the sole determinant of the relative efficacy for glutamate receptors. In addition, these studies have focused on the GluR2 subunit, which is the specific target of a physiologically important RNA-editing modification in vivo. We therefore sought to test the generality of the cleft closure-efficacy correlation for other AMPA-R subunits. Here, we present crystal structures of the GluR4(flip) LBD in complex with both full and partial agonists. As for GluR2, both agonists stabilize a closed-cleft conformation, and the partial agonist induces a smaller cleft closure than the full agonist. However, a detailed analysis of LBD-kainate interactions reveals the importance of subtle backbone conformational changes in the ligand-binding pocket in determining the magnitude of agonist-associated conformational changes. Furthermore, the GluR4 subunit exhibits a different correlation between receptor activation and LBD cleft closure than does GluR2.
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===Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate===
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Correlating AMPA receptor activation and cleft closure across subunits: crystal structures of the GluR4 ligand-binding domain in complex with full and partial agonists.,Gill A, Birdsey-Benson A, Jones BL, Henderson LP, Madden DR Biochemistry. 2008 Dec 30;47(52):13831-41. PMID:19102704<ref>PMID:19102704</ref>
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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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<div class="pdbe-citations 3en3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19102704}}, adds the Publication Abstract to the page
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19102704 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19102704}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Buffalo rat]]
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3EN3 is a 1 chain structure of 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=3EN3 OCA].
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[[Category: Large Structures]]
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[[Category: Gill, A]]
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==Reference==
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[[Category: Madden, D R]]
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<ref group="xtra">PMID:19102704</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
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[[Category: Gill, A.]]
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[[Category: Madden, D R.]]
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[[Category: Alternative splicing]]
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[[Category: Ampa receptor]]
[[Category: Ampa receptor]]
[[Category: Cell junction]]
[[Category: Cell junction]]
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[[Category: Lipoprotein]]
[[Category: Lipoprotein]]
[[Category: Membrane protein]]
[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 20 17:15:09 2009''
 

Current revision

Crystal Structure of the GluR4 Ligand-Binding domain in complex with kainate

PDB ID 3en3

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