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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.==
<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [https://pdbe.org/1jwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [https://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [https://pdbe.org/1jwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [https://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jwd ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jwd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
*[[S100 proteins 3D structures|S100 proteins 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: European rabbit]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chazin, W J]]
[[Category: Oryctolagus cuniculus]]
[[Category: Maler, L]]
[[Category: Chazin WJ]]
[[Category: Sastry, M]]
[[Category: Maler L]]
[[Category: Ef-hand]]
[[Category: Sastry M]]
[[Category: Metal binding protein]]
[[Category: S100 protein]]
[[Category: S100a6]]

Revision as of 10:55, 3 April 2024

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.

Structural highlights

1jwd is a 2 chain structure with sequence from Oryctolagus cuniculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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