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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6647
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pubmed:dateCreated |
1997-10-1
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pubmed:databankReference | |
pubmed:abstractText |
Many eukaryotic cellular and viral proteins have a covalently attached myristoyl group at the amino terminus. One such protein is recoverin, a calcium sensor in retinal rod cells, which controls the lifetime of photoexcited rhodopsin by inhibiting rhodopsin kinase. Recoverin has a relative molecular mass of 23,000 (M[r] 23K), and contains an amino-terminal myristoyl group (or related acyl group) and four EF hands. The binding of two Ca2+ ions to recoverin leads to its translocation from the cytosol to the disc membrane. In the Ca2+-free state, the myristoyl group is sequestered in a deep hydrophobic box, where it is clamped by multiple residues contributed by three of the EF hands. We have used nuclear magnetic resonance to show that Ca2+ induces the unclamping and extrusion of the myristoyl group, enabling it to interact with a lipid bilayer membrane. The transition is also accompanied by a 45-degree rotation of the amino-terminal domain relative to the carboxy-terminal domain, and many hydrophobic residues are exposed. The conservation of the myristoyl binding site and two swivels in recoverin homologues from yeast to humans indicates that calcium-myristoyl switches are ancient devices for controlling calcium-sensitive processes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hippocalcin,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recoverin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
389
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
198-202
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9296500-Calcium,
pubmed-meshheading:9296500-Calcium-Binding Proteins,
pubmed-meshheading:9296500-Crystallography, X-Ray,
pubmed-meshheading:9296500-Escherichia coli,
pubmed-meshheading:9296500-Eye Proteins,
pubmed-meshheading:9296500-Hippocalcin,
pubmed-meshheading:9296500-Lipoproteins,
pubmed-meshheading:9296500-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9296500-Models, Molecular,
pubmed-meshheading:9296500-Myristic Acids,
pubmed-meshheading:9296500-Nerve Tissue Proteins,
pubmed-meshheading:9296500-Protein Conformation,
pubmed-meshheading:9296500-Recombinant Proteins,
pubmed-meshheading:9296500-Recoverin
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pubmed:year |
1997
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pubmed:articleTitle |
Molecular mechanics of calcium-myristoyl switches.
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pubmed:affiliation |
Department of Neurobiology, Stanford University School of Medicine, California 94305, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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