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1dvi

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Revision as of 15:15, 25 December 2014

CALPAIN DOMAIN VI WITH CALCIUM BOUND

Structural highlights

1dvi is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	CAPN4 (Rattus norvegicus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CPNS1_RAT] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Evolutionary Conservation

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

Publication Abstract from PubMed

The crystal structure of a Ca(2+)-binding domain (dVI) of rat m-calpain has been determined at 2.3 A resolution, both with and without bound Ca2+. The structures reveal a unique fold incorporating five EF-hand motifs per monomer, three of which bind calcium at physiological calcium concentrations, with one showing a novel EF-hand coordination pattern. This investigation gives us a first view of the calcium-induced conformational changes, and consequently an insight into the mechanism of calcium induced activation in calpain. The crystal structures reveal a dVI homodimer which provides a preliminary model for the subunit dimerization in calpain.

Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes.,Blanchard H, Grochulski P, Li Y, Arthur JS, Davies PL, Elce JS, Cygler M Nat Struct Biol. 1997 Jul;4(7):532-8. PMID:9228945^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Blanchard H, Grochulski P, Li Y, Arthur JS, Davies PL, Elce JS, Cygler M. Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes. Nat Struct Biol. 1997 Jul;4(7):532-8. PMID:9228945

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dvi"

@@ Line 7: / Line 7: @@
 <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=1dvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dvi RCSB], [http://www.ebi.ac.uk/pdbsum/1dvi PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CPNS1_RAT CPNS1_RAT]] Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1dvi

From Proteopedia

Revision as of 15:15, 25 December 2014

CALPAIN DOMAIN VI WITH CALCIUM BOUND

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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