1avs

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<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=1avs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1avs RCSB], [http://www.ebi.ac.uk/pdbsum/1avs PDBsum]</span></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=1avs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1avs RCSB], [http://www.ebi.ac.uk/pdbsum/1avs PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 21:26, 25 December 2014

X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C

1avs, resolution 1.75Å

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