1iku
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(New page: 200px<br /><applet load="1iku" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iku" /> '''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE ...)
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Revision as of 15:21, 20 November 2007
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MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES
Overview
Recoverin, a retinal calcium-binding protein of relative molecular mass, (M(r)) 23K, participates in the recovery phase of visual excitation and in, adaptation to background light. The Ca(2+)-bound form of recoverin, prolongs the photoresponse, probably by blocking phosphorylation of, photoexcited rhodopsin. Retinal recoverin contains a covalently attached, myristoyl group or related acyl group at its amino terminus and two, Ca(2+)-binding sites. Ca2+ binding to myristoylated, but not, unmyristoylated, recoverin induces its translocation to bilayer membranes, indicating that the myristoyl group is essential to the read-out of, calcium signals (calcium-myristoyl switch). Here we present the solution, structure of Ca(2+)-free, myristoylated recombinant recoverin obtained by, heteronuclear multidimensional NMR spectroscopy. The myristoyl group is, sequestered in a deep hydrophobic pocket formed by many aromatic and other, hydrophobic residues from five flanking helices.
About this Structure
1IKU is a Single protein structure of sequence from Bos taurus with MYR as ligand. Full crystallographic information is available from OCA.
Reference
Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state., Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M, Nature. 1995 Aug 3;376(6539):444-7. PMID:7630423
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