1iku: Difference between revisions
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'''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES''' | '''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES''' | ||
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[[Category: Stryer, L.]] | [[Category: Stryer, L.]] | ||
[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
[[Category: | [[Category: Calcium-myristoyl switch]] | ||
[[Category: | [[Category: Calcuim-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:06:37 2008'' | |||
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Revision as of 20:06, 2 May 2008
MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES
OverviewOverview
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 StructureAbout this Structure
1IKU is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 20:06:37 2008