1iku: Difference between revisions
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[[Image:1iku.jpg|left|200px]] | [[Image:1iku.jpg|left|200px]] | ||
'''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES''' | {{Structure | ||
|PDB= 1iku |SIZE=350|CAPTION= <scene name='initialview01'>1iku</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MYR:MYRISTIC ACID'>MYR</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IKU is a [ | 1IKU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKU OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7630423 7630423] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcuim-binding protein]] | [[Category: calcuim-binding protein]] | ||
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Revision as of 12:51, 20 March 2008
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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
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