4f4l

</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=4f4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4l OCA], [https://pdbe.org/4f4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f4l RCSB], [https://www.ebi.ac.uk/pdbsum/4f4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f4l ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Voltage-gated sodium channels are vital membrane proteins essential for electrical signalling; in humans, they are key targets for the development of pharmaceutical drugs. Here we report the crystal structure of an open-channel conformation of NavMs, the bacterial channel pore from the marine bacterium Magnetococcus sp. (strain MC-1). It differs from the recently published crystal structure of a closed form of a related bacterial sodium channel (NavAb) by having its internal cavity accessible to the cytoplasmic surface as a result of a bend/rotation about a central residue in the carboxy-terminal transmembrane segment. This produces an open activation gate of sufficient diameter to allow hydrated sodium ions to pass through. Comparison of the open and closed structures provides new insight into the features of the functional states present in the activation cycles of sodium channels and the mechanism of channel opening and closing.

Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing.,McCusker EC, Bagneris C, Naylor CE, Cole AR, D'Avanzo N, Nichols CG, Wallace BA Nat Commun. 2012 Oct 2;3:1102. doi: 10.1038/ncomms2077. PMID:23033078<ref>PMID:23033078</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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