1cmf

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[[Image:1cmf.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmf OCA], [http://www.ebi.ac.uk/pdbsum/1cmf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cmf RCSB]</span>
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'''NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN'''
'''NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN'''
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[[Category: Thulin, E.]]
[[Category: Thulin, E.]]
[[Category: Waltho, J P.]]
[[Category: Waltho, J P.]]
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[[Category: calcium-binding protein]]
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[[Category: Calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:28 2008''
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Revision as of 09:53, 2 May 2008

Image:1cmf.gif

Template:STRUCTURE 1cmf

NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN


Overview

We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.

About this Structure

1CMF is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Calcium-induced structural changes and domain autonomy in calmodulin., Finn BE, Evenas J, Drakenberg T, Waltho JP, Thulin E, Forsen S, Nat Struct Biol. 1995 Sep;2(9):777-83. PMID:7552749 Page seeded by OCA on Fri May 2 12:53:27 2008

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