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New page: left|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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[[Image:1iku.jpg|left|200px]]<br /><applet load="1iku" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1iku.jpg|left|200px]]<br /><applet load="1iku" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1iku" />
caption="1iku" />
'''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES'''<br />
'''MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 STRUCTURES'''<br />


==Overview==
==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.
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==
==About this Structure==
1IKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MYR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IKU OCA].  
1IKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKU OCA].  


==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ames, J.B.]]
[[Category: Ames, J B.]]
[[Category: Harvey, T.S.]]
[[Category: Harvey, T S.]]
[[Category: Ikura, M.]]
[[Category: Ikura, M.]]
[[Category: Stryer, L.]]
[[Category: Stryer, L.]]
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[[Category: calcuim-binding protein]]
[[Category: calcuim-binding protein]]


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Revision as of 11:12, 21 February 2008

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1iku

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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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