1vp6: Difference between revisions

Revision as of 16:57, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1vp6.png

Template:STRUCTURE 1vp6

M.loti ion channel cylic nucleotide binding domainM.loti ion channel cylic nucleotide binding domain

Template:ABSTRACT PUBMED 15550244

About this StructureAbout this Structure

1VP6 is a Single protein structure of sequence from Mesorhizobium loti. This structure supersedes the now removed PDB entry 1pf0. Full crystallographic information is available from OCA.

ReferenceReference

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 Sun Jul 27 16:57:36 2008

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OCA

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-'''M.loti ion channel cylic nucleotide binding domain'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15550244}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15550244}}
 ==About this Structure==
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 [[Category: Silverman, W R.]]
 [[Category: Dimer helical bundle beta barrel core with cyclic amp bound]]
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