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Cited by 163

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Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearest-neighbors genetic algorithm

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Raymer, Michael L., Sanschagrin, Paul C., Punch, William F., Venkataraman, Sridhar, Goodman, Erik D., Kuhn, Leslie A.·1997·Journal of Molecular Biology

Abstract

Water-mediated ligand interactions are essential to biological processes, from product displacement in thymidylate synthase to DNA recognition by Trp repressor, yet the structural chemistry influencing whether bound water is displaced or participates in ligand binding is not well characterized. Consolv, employing a hybrid k-nearest-neighbors classifier/genetic algorithm, predicts bound water molecules conserved between free and ligand-bound protein structures by examining the environment of each water molecule in the free structure. Four environmental features are used: the water molecule's crystallographic temperature factor, the number of hydrogen bonds between the water molecule and protein, and the density and hydrophilicity of neighboring protein atoms. After training on 13 non-homologous proteins, Consolv predicted the conservation of active-site water molecules upon ligand binding with 75% accuracy (Matthews coefficient Cm = 0.41) for seven new proteins. Mispredictions typically involved water molecules predicted to be conserved that were displaced by a polar ligand atom, indicating that Consolv correctly assesses polar binding sites; 90% accuracy (Cm = 0.78) was achieved for predicting conserved active-site water or polar ligand atom binding. Consolv thus provides an accurate means for optimizing ligand design by identifying sites favored to be occupied by either a mediating water molecule or a polar ligand atom, as well as water molecules likely to be displaced by the ligand. Accuracy for predicting first-shell water conservation between independently determined structures was 61% (Cm=0.23). The ability to predict water-mediated and polar interactions from the free protein structure indicates the surprising extent to which the conservation or displacement of active-site bound water is independent of the ligand, and shows that the protein micro-environment of each water molecule is the dominant influence.

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Metadata

Authors
Raymer, M. L., Sanschagrin, P. C., Punch, W. F., Venkataraman, S., Goodman, E. D., & Kuhn, L. A.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
1997-01
Volume
265
Issue
4
Pages
445-464
ISSN
0022-2836 (ISSN-L)
OpenAlex
W2121954997
Cited by
163
References
1
FWCI
2.02
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearest-neighbors genetic algorithm. https://app.cochat.ai/papers/10.1006/jmbi.1996.0746
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Raymer, M. L., Sanschagrin, P. C., Punch, W. F., Venkataraman, S., Goodman, E. D., & Kuhn, L. A. (1997). Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearest-neighbors genetic algorithm. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.1996.0746

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