1jwd: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])
|GENE= R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])
|DOMAIN=
|RELATEDENTRY=[[1a03|1A03]], [[2cnp|2CNP]], [[1cnp|1CNP]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB]</span>
}}
}}


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[[Category: s100a6]]
[[Category: s100a6]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:23 2008''
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Revision as of 21:40, 30 March 2008

File:1jwd.gif


PDB ID 1jwd

Drag the structure with the mouse to rotate
Gene: R-S100A6 (Oryctolagus cuniculus)
Related: 1A03, 2CNP, 1CNP


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.


OverviewOverview

Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.

About this StructureAbout this Structure

1JWD is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin., Maler L, Sastry M, Chazin WJ, J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:11902843

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