1dmo

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|ACTIVITY=
|ACTIVITY=
|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
|GENE= XENOPUS LAEVIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmo OCA], [http://www.ebi.ac.uk/pdbsum/1dmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dmo RCSB]</span>
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[[Category: calcium-induced conformational change]]
[[Category: calcium-induced conformational change]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:40:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:44:48 2008''

Revision as of 16:44, 30 March 2008


PDB ID 1dmo

Drag the structure with the mouse to rotate
Gene: XENOPUS LAEVIS (Xenopus laevis)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CALMODULIN, NMR, 30 STRUCTURES


Overview

The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.

About this Structure

1DMO is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.

Reference

Calcium-induced conformational transition revealed by the solution structure of apo calmodulin., Zhang M, Tanaka T, Ikura M, Nat Struct Biol. 1995 Sep;2(9):758-67. PMID:7552747

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