1q5o: Difference between revisions

Revision as of 13:29, 28 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:1q5o.png

Template:STRUCTURE 1q5o

HCN2J 443-645 in the presence of cAMP, selenomethionine derivativeHCN2J 443-645 in the presence of cAMP, selenomethionine derivative

Template:ABSTRACT PUBMED 12968185

About this StructureAbout this Structure

1Q5O is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for modulation and agonist specificity of HCN pacemaker channels., Zagotta WN, Olivier NB, Black KD, Young EC, Olson R, Gouaux E, Nature. 2003 Sep 11;425(6954):200-5. PMID:12968185

Page seeded by OCA on Mon Jul 28 13:29:50 2008

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OCA

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-'''HCN2J 443-645 in the presence of cAMP, selenomethionine derivative'''
+===HCN2J 443-645 in the presence of cAMP, selenomethionine derivative===
-==Overview==
+<!--
-The family of hyperpolarization-activated, cyclic nucleotide-modulated (HCN) channels are crucial for a range of electrical signalling, including cardiac and neuronal pacemaker activity, setting resting membrane electrical properties and dendritic integration. These nonselective cation channels, underlying the I(f), I(h) and I(q) currents of heart and nerve cells, are activated by membrane hyperpolarization and modulated by the binding of cyclic nucleotides such as cAMP and cGMP. The cAMP-mediated enhancement of channel activity is largely responsible for the increase in heart rate caused by beta-adrenergic agonists. Here we have investigated the mechanism underlying this modulation by studying a carboxy-terminal fragment of HCN2 containing the cyclic nucleotide-binding domain (CNBD) and the C-linker region that connects the CNBD to the pore. X-ray crystallographic structures of this C-terminal fragment bound to cAMP or cGMP, together with equilibrium sedimentation analysis, identify a tetramerization domain and the mechanism for cyclic nucleotide specificity, and suggest a model for ligand-dependent channel modulation. On the basis of amino acid sequence similarity to HCN channels, the cyclic nucleotide-gated, and eag- and KAT1-related families of channels are probably related to HCN channels in structure and mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_12968185}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12968185 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12968185}}
 ==About this Structure==
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 [[Category: Pacemaker]]
 [[Category: Pka]]
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