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1h67
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(Difference between revisions)
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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=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [http://www.ebi.ac.uk/pdbsum/1h67 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=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [http://www.ebi.ac.uk/pdbsum/1h67 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CNN1_CHICK CNN1_CHICK]] Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 15:19, 25 December 2014
NMR STRUCTURE OF THE CH DOMAIN OF CALPONIN
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