4g80: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:


==Crystal structure of voltage sensing domain of Ci-VSP with fragment antibody (WT, 3.8 A)==
==Crystal structure of voltage sensing domain of Ci-VSP with fragment antibody (WT, 3.8 A)==
<StructureSection load='4g80' size='340' side='right' caption='[[4g80]], [[Resolution|resolution]] 3.58&Aring;' scene=''>
<StructureSection load='4g80' size='340' side='right'caption='[[4g80]], [[Resolution|resolution]] 3.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g80]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascidia_intestinalis Ascidia intestinalis] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G80 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g80]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ciona_intestinalis Ciona intestinalis] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G80 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g7y|4g7y]], [[4g7v|4g7v]]</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]] 3.58&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ci-VSP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7719 Ascidia intestinalis])</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=4g80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g80 OCA], [https://pdbe.org/4g80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g80 RCSB], [https://www.ebi.ac.uk/pdbsum/4g80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g80 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=4g80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g80 OCA], [http://pdbe.org/4g80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g80 RCSB], [http://www.ebi.ac.uk/pdbsum/4g80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g80 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F6XHE4_CIOIN F6XHE4_CIOIN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The transduction of transmembrane electric fields into protein motion has an essential role in the generation and propagation of cellular signals. Voltage-sensing domains (VSDs) carry out these functions through reorientations of positive charges in the S4 helix. Here, we determined crystal structures of the Ciona intestinalis VSD (Ci-VSD) in putatively active and resting conformations. S4 undergoes an ~5-A displacement along its main axis, accompanied by an ~60 degrees rotation. This movement is stabilized by an exchange in countercharge partners in helices S1 and S3 that generates an estimated net charge transfer of ~1 eo. Gating charges move relative to a ''hydrophobic gasket' that electrically divides intra- and extracellular compartments. EPR spectroscopy confirms the limited nature of S4 movement in a membrane environment. These results provide an explicit mechanism for voltage sensing and set the basis for electromechanical coupling in voltage-dependent enzymes and ion channels.
Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain.,Li Q, Wanderling S, Paduch M, Medovoy D, Singharoy A, McGreevy R, Villalba-Galea CA, Hulse RE, Roux B, Schulten K, Kossiakoff A, Perozo E Nat Struct Mol Biol. 2014 Mar;21(3):244-52. doi: 10.1038/nsmb.2768. Epub 2014 Feb, 2. PMID:24487958<ref>PMID:24487958</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4g80" style="background-color:#fffaf0;"></div>
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[3D structures of human antibody|3D structures of human antibody]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ascidia intestinalis]]
[[Category: Ciona intestinalis]]
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Li, Q]]
[[Category: Large Structures]]
[[Category: Alpha helix]]
[[Category: Li Q]]
[[Category: Fragment antibody]]
[[Category: Membrane protein]]
[[Category: Sensing voltage]]
[[Category: Voltage sensing domain]]
Retrieved from "https://proteopedia.org/4g80"