1jwd
From Proteopedia
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| - | [[Image:1jwd.gif|left|200px]] | + | [[Image:1jwd.gif|left|200px]] |
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| - | '''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.''' | + | {{Structure |
| + | |PDB= 1jwd |SIZE=350|CAPTION= <scene name='initialview01'>1jwd</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus]) | ||
| + | }} | ||
| + | |||
| + | '''Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JWD is a [ | + | 1JWD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11902843 11902843] |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: s100a6]] | [[Category: s100a6]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:23 2008'' |
Revision as of 10:09, 20 March 2008
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| Gene: | R-S100A6 (Oryctolagus cuniculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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