1cmf
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(New page: 200px<br /><applet load="1cmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmf" /> '''NMR SOLUTION STRUCTURE OF APO CALMODULIN CAR...)
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Revision as of 10:27, 20 November 2007
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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
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