1omr: Difference between revisions

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[[Image:1omr.gif|left|200px]]
[[Image:1omr.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1omr", creates the "Structure Box" on the page.
|SITE=
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|GENE= RCV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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|DOMAIN=
{{STRUCTURE_1omr| PDB=1omr  | SCENE= }}  
|RELATEDENTRY=[[1omv|1OMV]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1omr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omr OCA], [http://www.ebi.ac.uk/pdbsum/1omr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1omr RCSB]</span>
}}


'''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3'''
'''non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3'''
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[[Category: Granzin, J.]]
[[Category: Granzin, J.]]
[[Category: Weiergraber, O H.]]
[[Category: Weiergraber, O H.]]
[[Category: ef-hand]]
[[Category: Ef-hand]]
[[Category: helix-loop-helix]]
[[Category: Helix-loop-helix]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:02:25 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:26 2008''

Revision as of 04:02, 3 May 2008

File:1omr.gif

Template:STRUCTURE 1omr

non-myristoylated wild-type bovine recoverin with calcium bound to EF-hand 3


OverviewOverview

Recoverin is a Ca2+-regulated signal transduction modulator found in vertebrate retina that has been shown to undergo dramatic conformational changes upon Ca2+ binding to its two functional EF-hand motifs. To elucidate the differential impact of the N-terminal myristoylation as well as occupation of the two Ca2+ binding sites on recoverin structure and function, we have investigated a non-myristoylated E85Q mutant exhibiting virtually no Ca2+ binding to EF-2. Crystal structures of the mutant protein as well as the non-myristoylated wild-type have been determined. Although the non-myristoylated E85Q mutant does not display any functional activity, its three-dimensional structure in the presence of Ca2+ resembles the myristoylated wild-type with two Ca2+ but is quite dissimilar from the myristoylated E85Q mutant. We conclude that the N-terminal myristoyl modification significantly stabilizes the conformation of the Ca2+-free protein (i.e. the T conformation) during the stepwise transition toward the fully Ca2+-occupied state. On the basis of these observations, a refined model for the role of the myristoyl group as an intrinsic allosteric modulator is proposed.

About this StructureAbout this Structure

1OMR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Impact of N-terminal myristoylation on the Ca2+-dependent conformational transition in recoverin., Weiergraber OH, Senin II, Philippov PP, Granzin J, Koch KW, J Biol Chem. 2003 Jun 20;278(25):22972-9. Epub 2003 Apr 9. PMID:12686556 Page seeded by OCA on Sat May 3 04:02:25 2008

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