The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearest-neighbors genetic algorithm
Open accessAbstract
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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Citations
Cites
Comparison of the predicted and observed secondary structure of T4 phage lysozyme
Matthews, B. W. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90109-9 · Cited by 5,399 · cited 2×
“…ways: by the number of correctly predicted water sites out of the total number of evaluated sites (percentage accuracy), by the percentage accuracy for each class (conserved, displaced), and by the Matthews coefficient Cm, which assesses the balance of accuracy between classes (Matthews, 1975).”
BackgroundMethod
Cited by
Zheng, W., & Tropsha, A. (2000) · Journal of Chemical Information and Computer Sciences · doi:10.1021/ci980033m · Cited by 450
Modeling water molecules in protein-ligand docking using GOLD.
Verdonk, M. L., Chessari, G., Cole, J. C., Hartshorn, M. J., Murray, C. W., Nissink, J. W. M., Taylor, R. D., & Taylor, R. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050543p · Cited by 393
Flexible docking using tabu search and an empirical estimate of binding affinity
Baxter, C. A., Murray, C. W., Clark, D. E., Westhead, D. R., & Eldridge, M. D. (1998) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19981115)33:3<367::aid-prot6>3.0.co;2-w · Cited by 375
A Force Field with Discrete Displaceable Waters and Desolvation Entropy for Hydrated Ligand Docking
Forli, S., & Olson, A. J. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm2005145 · Cited by 290
Orientational disorder and entropy of water in protein cavities
Denisov, V. P., Venu, K., Peters, J., Hörlein, H. D., & Halle, B. (1997) · The Journal of Physical Chemistry B · doi:10.1021/jp9712213 · Cited by 108
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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- 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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