1tnh
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(New page: 200px<br /><applet load="1tnh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tnh, resolution 1.8Å" /> '''PREDICTION OF NOVEL S...)
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Revision as of 01:18, 21 November 2007
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PREDICTION OF NOVEL SERINE PROTEASE INHIBITORS
Overview
We describe here the use of a rapid computational method to predict the, relative binding strengths of a series of small-molecule ligands for the, serine proteinase trypsin. Flexible molecular models of the ligands were, docked to the proteinase using an all-atom potential set, without cutoff, limits for the non-bonded and electrostatic energies. The binding-strength, calculation is done directly in terms of a molecular mechanics potential., The binding of eighteen different compounds, including non-binding, controls, has been successfully predicted. The measured Ki is correlated, with the predicted energy. The correctness of the theoretical calculations, is demonstrated with both kinetics measurements and X-ray structure, determination of six enzyme-inhibitor complexes.
About this Structure
1TNH is a Single protein structure of sequence from Bos taurus with CA and FBA as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Prediction of new serine proteinase inhibitors., Kurinov IV, Harrison RW, Nat Struct Biol. 1994 Oct;1(10):735-43. PMID:7634078
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