View source for 4g80


==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=''>
== Structural highlights ==
<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='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='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>
</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__
</StructureSection>
[[Category: Ciona intestinalis]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Li Q]]