Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0097-8485(02)00050-5
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dc.titleCLiBE: A database of computed ligand binding energy for ligand-receptor complexes
dc.contributor.authorChen, X.
dc.contributor.authorJi, Z.L.
dc.contributor.authorZhi, D.G.
dc.contributor.authorChen, Y.Z.
dc.date.accessioned2014-10-27T08:23:55Z
dc.date.available2014-10-27T08:23:55Z
dc.date.issued2002-11-01
dc.identifier.citationChen, X., Ji, Z.L., Zhi, D.G., Chen, Y.Z. (2002-11-01). CLiBE: A database of computed ligand binding energy for ligand-receptor complexes. Computers and Chemistry 26 (6) : 661-666. ScholarBank@NUS Repository. https://doi.org/10.1016/S0097-8485(02)00050-5
dc.identifier.issn00978485
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100269
dc.description.abstractConsideration of binding competitiveness of a drug candidate against natural ligands and other drugs that bind to the same receptor site may facilitate the rational development of a candidate into a potent drug. A strategy that can be applied to computer-aided drug design is to evaluate ligand-receptor interaction energy or other scoring functions of a designed drug with that of the relevant ligands known to bind to the same binding site. As a tool to facilitate such a strategy, a database of ligand-receptor interaction energy is developed from known ligand-receptor 3D structural entries in the Protein Databank (PDB). The Energy is computed based on a molecular mechanics force field that has been used in the prediction of therapeutic and toxicity targets of drugs. This database also contains information about ligand function and other properties and it can be accessed at http://xin.cz3.nus.edu.sg/group/CLiBE.asp. The computed energy components may facilitate the probing of the mode of action and other profiles of binding. A number of computed energies of some PDB ligand-receptor complexes in this database are studied and compared to experimental binding affinity. A certain degree of correlation between the computed energy and experimental binding affinity is found, which suggests that the computed energy may be useful in facilitating a qualitative analysis of drug binding competitiveness. © 2002 Elsevier Science Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0097-8485(02)00050-5
dc.sourceScopus
dc.subjectComputer-aided drug design
dc.subjectDrug competitive binding
dc.subjectLigand function and property
dc.subjectLigand-receptor interaction energy
dc.typeArticle
dc.contributor.departmentCOMPUTATIONAL SCIENCE
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/S0097-8485(02)00050-5
dc.description.sourcetitleComputers and Chemistry
dc.description.volume26
dc.description.issue6
dc.description.page661-666
dc.description.codenCOCHD
dc.identifier.isiut000178479600008
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