1jwd

<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a03|1a03]], [[2cnp|2cnp]], [[1cnp|1cnp]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>

[[https://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11902843</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: European rabbit]]

[[Category: Chazin, W J]]

[[Category: Maler, L]]

[[Category: Sastry, M]]

[[Category: Ef-hand]]

[[Category: S100a6]]