2f3y: Difference between revisions

Revision as of 11:20, 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:2f3y.png

Template:STRUCTURE 2f3y

Calmodulin/IQ domain complexCalmodulin/IQ domain complex

Template:ABSTRACT PUBMED 16338416

About this StructureAbout this Structure

2F3Y is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel., Fallon JL, Halling DB, Hamilton SL, Quiocho FA, Structure. 2005 Dec;13(12):1881-6. PMID:16338416

Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex., Meador WE, Means AR, Quiocho FA, Science. 1992 Aug 28;257(5074):1251-5. PMID:1519061

A closed compact structure of native Ca(2+)-calmodulin., Fallon JL, Quiocho FA, Structure. 2003 Oct;11(10):1303-7. PMID:14527397

Page seeded by OCA on Mon Jul 28 11:20:29 2008

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

OCA

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-[[Image:2f3y.gif|left|200px]]
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 {{STRUCTURE_2f3y|  PDB=2f3y  |  SCENE=  }}
-'''Calmodulin/IQ domain complex'''
+===Calmodulin/IQ domain complex===
-==Overview==
+<!--
-Ca2+-dependent inactivation (CDI) and facilitation (CDF) of the Ca(v)1.2 Ca2+ channel require calmodulin binding to a putative IQ motif in the carboxy-terminal tail of the pore-forming subunit. We present the 1.45 A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v)1.2. This structure shows that parallel binding of calmodulin to the IQ domain is governed by hydrophobic interactions. Mutations of residues I1672 and Q1673 in the peptide to alanines, which abolish CDI but not CDF in the channel, do not greatly alter the structure. Both lobes of Ca2+-saturated CaM bind to the IQ peptide but isoleucine 1672, thought to form an intramolecular interaction that drives CDI, is buried. These findings suggest that this structure could represent the conformation that calmodulin assumes in CDF.
+The line below this paragraph, {{ABSTRACT_PUBMED_16338416}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16338416 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16338416}}
 ==About this Structure==
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 ==Reference==
 Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel., Fallon JL, Halling DB, Hamilton SL, Quiocho FA, Structure. 2005 Dec;13(12):1881-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16338416 16338416]
+Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex., Meador WE, Means AR, Quiocho FA, Science. 1992 Aug 28;257(5074):1251-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1519061 1519061]
+A closed compact structure of native Ca(2+)-calmodulin., Fallon JL, Quiocho FA, Structure. 2003 Oct;11(10):1303-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527397 14527397]
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
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 [[Category: Cav1 2]]
 [[Category: Iq domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:26:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:20:29 2008''