4i9w
From Proteopedia
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| - | + | ==Human two pore domain K+ channel TRAAK (K2P4.1) - Fab complex structure== | |
| - | + | <StructureSection load='4i9w' size='340' side='right' caption='[[4i9w]], [[Resolution|resolution]] 2.75Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4i9w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I9W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">K2P4.1, KCNK4, TRAAK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4i9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i9w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i9w RCSB], [http://www.ebi.ac.uk/pdbsum/4i9w PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | TRAAK (TWIK-related arachidonic acid-stimulated K(+) channel, K2P4.1) K(+) ion channels are expressed predominantly in the nervous system to control cellular resting membrane potential and are regulated by mechanical and chemical properties of the lipid membrane. TRAAK channels are twofold symmetric, which precludes a direct extension of gating mechanisms that close canonical fourfold symmetric K(+) channels. We present the crystal structure of human TRAAK in complex with antibody antigen-binding fragments (Fabs) at 2.75-A resolution. In contrast to a previous structure, this structure reveals a domain-swapped chain connectivity enabled by the helical cap that exchanges two opposing outer helices 180 degrees around the channel. An unrelated conformational change of an inner helix seals a side opening to the membrane bilayer and is associated with structural changes around the K(+)-selectivity filter that may have implications for mechanosensitivity and gating of TRAAK channels. | ||
| - | + | Domain-swapped chain connectivity and gated membrane access in a Fab-mediated crystal of the human TRAAK K+ channel.,Brohawn SG, Campbell EB, Mackinnon R Proc Natl Acad Sci U S A. 2013 Feb 5;110(6):2129-34. doi:, 10.1073/pnas.1218950110. Epub 2013 Jan 22. PMID:23341632<ref>PMID:23341632</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[ | + | </div> |
| + | |||
| + | ==See Also== | ||
| + | *[[Antibody|Antibody]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Brohawn, S G | + | [[Category: Brohawn, S G]] |
| - | [[Category: Mackinnon, R | + | [[Category: Mackinnon, R]] |
[[Category: Metal transport]] | [[Category: Metal transport]] | ||
[[Category: Potassium ion channel]] | [[Category: Potassium ion channel]] | ||
Revision as of 13:07, 21 December 2014
Human two pore domain K+ channel TRAAK (K2P4.1) - Fab complex structure
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