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1avs
From Proteopedia
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(New page: 200px<br /><applet load="1avs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avs, resolution 1.75Å" /> '''X-RAY CRYSTALLOGRAPH...)
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Revision as of 09:02, 20 November 2007
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X-RAY CRYSTALLOGRAPHIC STUDY OF CALCIUM-SATURATED N-TERMINAL DOMAIN OF TROPONIN C
Overview
We have solved and refined the crystal and molecular structures of the, calcium-saturated N-terminal domain of troponin C (TnC) to 1.75 A, resolution. This has allowed for the first detailed analysis of the, calcium binding sites of this molecular switch in the calcium-loaded, state. The results provide support for the proposed binding order and, qualitatively, for the affinity of calcium in the two regulatory calcium, binding sites. Based on a comparison with the high-resolution apo-form of, TnC we propose a possible mechanism for the calcium-mediated exposure of a, large hydrophobic surface that is central to the initiation of muscle, contraction within the cell.
About this Structure
1AVS is a Single protein structure of sequence from Gallus gallus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 A resolution., Strynadka NC, Cherney M, Sielecki AR, Li MX, Smillie LB, James MN, J Mol Biol. 1997 Oct 17;273(1):238-55. PMID:9367759
Page seeded by OCA on Tue Nov 20 11:09:52 2007
