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4cpv
From Proteopedia
(Difference between revisions)
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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=4cpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cpv RCSB], [http://www.ebi.ac.uk/pdbsum/4cpv 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=4cpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cpv RCSB], [http://www.ebi.ac.uk/pdbsum/4cpv PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PRVB_CYPCA PRVB_CYPCA]] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 08:24, 24 December 2014
REFINED CRYSTAL STRUCTURE OF CALCIUM-LIGANDED CARP PARVALBUMIN 4.25 AT 1.5-ANGSTROMS RESOLUTION
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