1vp6
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(New page: 200px<br /><applet load="1vp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vp6, resolution 1.70Å" /> '''M.loti ion channel c...)
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Revision as of 20:48, 24 November 2007
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M.loti ion channel cylic nucleotide binding domain
Overview
Here we describe the initial functional characterization of a cyclic, nucleotide regulated ion channel from the bacterium Mesorhizobium loti and, present two structures of its cyclic nucleotide binding domain, with and, without cAMP. The domains are organized as dimers with the interface, formed by the linker regions that connect the nucleotide binding pocket to, the pore domain. Together, structural and functional data suggest the, domains form two dimers on the cytoplasmic face of the channel. We propose, a model for gating in which ligand binding alters the structural, relationship within a dimer, directly affecting the position of the, adjacent transmembrane helices.
About this Structure
1VP6 is a Single protein structure of sequence from Mesorhizobium loti with BR and CMP as ligands. This structure superseeds the now removed PDB entry 1PF0. Full crystallographic information is available from OCA.
Reference
Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel., Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH, Cell. 2004 Nov 24;119(5):615-27. PMID:15550244
Page seeded by OCA on Sat Nov 24 22:55:32 2007
