2ogu: Difference between revisions

Revision as of 11:26, 29 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:2ogu.png

Template:STRUCTURE 2ogu

Crystal structure of the isolated MthK RCK domainCrystal structure of the isolated MthK RCK domain

Template:ABSTRACT PUBMED 17287352

About this StructureAbout this Structure

2OGU is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

Dynamic oligomeric conversions of the cytoplasmic RCK domains mediate MthK potassium channel activity., Kuo MM, Baker KA, Wong L, Choe S, Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2151-6. Epub 2007 Feb 7. PMID:17287352

Page seeded by OCA on Tue Jul 29 11:26:49 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of the isolated MthK RCK domain'''
+===Crystal structure of the isolated MthK RCK domain===
-==Overview==
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-The crystal structure of the RCK-containing MthK provides a molecular framework for understanding the ligand gating mechanisms of K+ channels. Here we examined the macroscopic currents of MthK in enlarged Escherichia coli membrane by patch clamp and rapid perfusion techniques and showed that the channel undergoes desensitization in seconds after activation by Ca2+ or Cd2+. Additionally, MthK is inactivated by slightly acidic pH only from the cytoplasmic side. Examinations of isolated RCK domain by size-exclusion chromatography, static light scattering, analytical sedimentation, and stopped-flow spectroscopy show that Ca2+ rapidly converts isolated RCK monomers to multimers at alkaline pH. In contrast, the RCK domain at acidic pH remains firmly dimeric regardless of Ca2+ but restores predominantly to multimer or monomer at basic pH with or without Ca2+, respectively. These functional and biochemical analyses correlate the four functional states of the MthK channel with distinct oligomeric states of its RCK domains and indicate that the RCK domains undergo oligomeric conversions in modulating MthK activities.
+The line below this paragraph, {{ABSTRACT_PUBMED_17287352}}, adds the Publication Abstract to the page
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