1jwd

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[[Image:1jwd.gif|left|200px]]
[[Image:1jwd.gif|left|200px]]
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{{Structure
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|PDB= 1jwd |SIZE=350|CAPTION= <scene name='initialview01'>1jwd</scene>
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The line below this paragraph, containing "STRUCTURE_1jwd", creates the "Structure Box" on the page.
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|GENE= R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])
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{{STRUCTURE_1jwd| PDB=1jwd | SCENE= }}
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|RELATEDENTRY=[[1a03|1A03]], [[2cnp|2CNP]], [[1cnp|1CNP]]
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|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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'''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.'''
'''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.'''
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[[Category: Maler, L.]]
[[Category: Maler, L.]]
[[Category: Sastry, M.]]
[[Category: Sastry, M.]]
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[[Category: ca(2+)-binding protein]]
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[[Category: Ef-hand]]
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[[Category: ef-hand]]
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[[Category: S100 protein]]
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[[Category: s100 protein]]
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[[Category: S100a6]]
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[[Category: s100a6]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:00:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:39:58 2008''
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Revision as of 19:00, 2 May 2008

Template:STRUCTURE 1jwd

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


Overview

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 Structure

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

Reference

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 Page seeded by OCA on Fri May 2 22:00:24 2008

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