1cta
From Proteopedia
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DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY
Overview
The solution structure of a 34-residue synthetic calcium-binding peptide, from site III of chicken troponin-C has been determined by 1H NMR, spectroscopy. In solution and in the presence of calcium this peptide, forms a symmetric two-site homodimeric calcium-binding domain (Shaw et, al., 1990). The solution structure of this dimer was determined from the, measurement of 470 NOEs from a 75-ms NOESY data set. For the dimer, structure determination, the constraint list included 868 distance, restraints, 44 phi angles, and 24 chi 1 and 2 chi 2 angles. Seven, structures were calculated by restrained molecular dynamics using a, procedure in which intramonomer distances were used first and then all, distances, intra- and intermonomer, were input during further dynamics., The structures exhibited a fold very similar to the C-terminal domain of, troponin-C comprised of a pair of helix-loop-helix calcium-binding sites., The rms deviation of these structures for backbone atoms between residues, 97-122 and 97'-122' for the dimer was 0.82 A. The dimer structure was also, calculated to be more symmetric than sites III and IV in troponin-C.
About this Structure
1CTA is a Single protein structure of sequence from [1] with CA, ACE and NH2 as ligands. Full crystallographic information is available from OCA.
Reference
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy., Shaw GS, Hodges RS, Sykes BD, Biochemistry. 1992 Oct 13;31(40):9572-80. PMID:1390738
Page seeded by OCA on Sun Nov 25 01:55:57 2007
Categories: Single protein | Shaw, G.S. | Sykes, B.D. | ACE | CA | NH2 | Muscle protein
