Quantitative measurement of protease ligand conformation |
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Authors: | Christopher J R Illingworth Kevin E B Parkes Christopher R Snell Christopher A Reynolds |
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Institution: | (1) Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK;(2) Medivir UK Ltd., Chesterford Research Park, Little Chesterford, Essex, CB10 1XL, UK |
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Abstract: | The tendency for protease ligands to bind in an extended conformation has been suggested as an important factor for the identification
of compounds of medicinal importance. Here we present a novel graph-theoretical method giving a quantitative measure of ligand
conformation, and through application of this method to a representative set of protease ligands in bound and unbound conformations,
derive the result that protease ligands are more extended in conformation when in their bound state.
Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. |
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Keywords: | Conformation Inhibitor Ligand Measurement Protease |
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