1omc
From Proteopedia
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SOLUTION STRUCTURE OF OMEGA-CONOTOXIN GVIA USING 2-D NMR SPECTROSCOPY AND RELAXATION MATRIX ANALYSIS
Overview
We report here the solution structure of omega-conotoxin GVIA, a peptide, antagonist of the N-type neuronal voltage-sensitive calcium channel. The, structure was determined using two-dimensional NMR in combination with, distance geometry and restrained molecular dynamics. The full relaxation, matrix analysis program MARDIGRAS was used to generate maximum and minimum, distance restraints from the crosspeak intensities in NOESY spectra. The, 187 restraints obtained were used in conjunction with 23 angle restraints, from vicinal coupling constants as input for the structure calculations., The backbones of the best 21 structures match with an average pairwise, RMSD of 0.58 A. The structures contain a short segment of triple-stranded, beta-sheet involving residues 6-8, 18-21, and 24-27, making this the, smallest published peptide structure to contain a triple-stranded, beta-sheet. Conotoxins have been shown to be effective neuroprotective, agents in animal models of brain ischemia. Our results should aid in the, design of novel nonpeptide compounds with potential therapeutic utility.
About this Structure
1OMC is a Single protein structure of sequence from Conus geographus with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of omega-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis., Davis JH, Bradley EK, Miljanich GP, Nadasdi L, Ramachandran J, Basus VJ, Biochemistry. 1993 Jul 27;32(29):7396-405. PMID:8338837
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