Abstract
As part of a program aimed at the design and synthesis of constrained MMP inhibitors, a survey of the reported X-ray and NMR structures of MMP/inhibitor complexes was performed, revealing mutations of key amino acids at different subsites between MMPs. A comparative study of fully automated docking programs AutoDock and DOCK in closely approximating the X-ray crystal structures of ten selected MMP inhibitors was performed. AutoDock proved to be highly reliable, efficient and predictive for a set of inhibitors with less than six atom types.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites / genetics
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Computer Simulation
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Crystallography, X-Ray
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Drug Design*
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In Vitro Techniques
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Macromolecular Substances
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Magnetic Resonance Spectroscopy
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Matrix Metalloproteinase Inhibitors*
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Matrix Metalloproteinases / chemistry
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Matrix Metalloproteinases / genetics
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Matrix Metalloproteinases / metabolism
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Models, Molecular
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Mutagenesis, Site-Directed
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Protease Inhibitors / chemistry*
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Protease Inhibitors / metabolism
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Protease Inhibitors / pharmacology*
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Software
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Thermodynamics
Substances
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Macromolecular Substances
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Matrix Metalloproteinase Inhibitors
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Protease Inhibitors
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Matrix Metalloproteinases