1cnp

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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB], [http://www.ebi.ac.uk/pdbsum/1cnp PDBsum]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cnp RCSB], [http://www.ebi.ac.uk/pdbsum/1cnp PDBsum]</span></td></tr>
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== Function ==
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[[http://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]]

Revision as of 14:22, 24 December 2014

THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD FOR S100 CA2+-BINDING PROTEINS, NMR, 22 STRUCTURES

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