4chv: Difference between revisions
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==The electron crystallography structure of the cAMP-bound potassium channel MloK1== | |||
<StructureSection load='4chv' size='340' side='right' caption='[[4chv]], [[Resolution|resolution]] 7.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4chv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33669 Atcc 33669]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4chw|4chw]]</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=4chv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4chv RCSB], [http://www.ebi.ac.uk/pdbsum/4chv PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1-S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an 'open' conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels. | |||
Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.,Kowal J, Chami M, Baumgartner P, Arheit M, Chiu PL, Rangl M, Scheuring S, Schroder GF, Nimigean CM, Stahlberg H Nat Commun. 2014 Jan 28;5:3106. doi: 10.1038/ncomms4106. PMID:24469021<ref>PMID:24469021</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Ion channels|Ion channels]] | |||
[[Category: Arheit, M | == References == | ||
[[Category: Baumgartner, P | <references/> | ||
[[Category: Chami, M | __TOC__ | ||
[[Category: Chiu, P L | </StructureSection> | ||
[[Category: Kowal, J | [[Category: Atcc 33669]] | ||
[[Category: Nimigean, C M | [[Category: Arheit, M]] | ||
[[Category: Rangl, M | [[Category: Baumgartner, P]] | ||
[[Category: Scheuring, S | [[Category: Chami, M]] | ||
[[Category: Schroeder, G F | [[Category: Chiu, P L]] | ||
[[Category: Stahlberg, H | [[Category: Kowal, J]] | ||
[[Category: Nimigean, C M]] | |||
[[Category: Rangl, M]] | |||
[[Category: Scheuring, S]] | |||
[[Category: Schroeder, G F]] | |||
[[Category: Stahlberg, H]] | |||
[[Category: 2d crystal]] | [[Category: 2d crystal]] | ||
[[Category: Cnbd]] | [[Category: Cnbd]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
[[Category: Voltage gated potassium channel]] | [[Category: Voltage gated potassium channel]] | ||
Revision as of 09:14, 25 December 2014
The electron crystallography structure of the cAMP-bound potassium channel MloK1
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