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dc.contributor.authorFirth-Clark, Stuart
dc.contributor.authorKirton, Stewart B.
dc.contributor.authorWillems, Henrite M. G.
dc.contributor.authorWilliams, Anthony
dc.date.accessioned2013-01-11T13:29:34Z
dc.date.available2013-01-11T13:29:34Z
dc.date.issued2008-02
dc.identifier.citationFirth-Clark , S , Kirton , S B , Willems , H M G & Williams , A 2008 , ' De novo ligand design to partially flexible active sites : Application of the Reflex algorithm to carboxypeptidase A, acetylcholinesterase, and the estrogen receptor ' , Journal of Chemical Information and Modeling , vol. 48 , no. 2 , pp. 296-305 . https://doi.org/10.1021/ci700282u
dc.identifier.issn1549-9596
dc.identifier.otherPURE: 942409
dc.identifier.otherPURE UUID: fd1fe441-05a3-4be2-a8bd-d063f9eb9cb6
dc.identifier.otherWOS: 000253428400007
dc.identifier.otherScopus: 41649095370
dc.identifier.urihttp://hdl.handle.net/2299/9578
dc.description.abstractReflex is a recent algorithm in the de novo ligand design software, SkelGen, that allows the flexibility of amino acid side chains in a protein to be taken into account during the drug-design process. In this paper the impact of flexibility on the solutions generated by the de novo design algorithm, when applied to carboxypeptidase A, acetylcholinesterase, and the estrogen receptor (ER), is investigated. The results for each of the targets indicate that when allowing side-chain movement in the active site, solutions are generated that were not accessible from the multiple static protein conformations available for these targets. Furthermore, an analysis of structures generated in a flexible versus a static ER active site suggests that these additional solutions are not merely noise but contain many interesting chemotypes.en
dc.format.extent10
dc.language.isoeng
dc.relation.ispartofJournal of Chemical Information and Modeling
dc.titleDe novo ligand design to partially flexible active sites : Application of the Reflex algorithm to carboxypeptidase A, acetylcholinesterase, and the estrogen receptoren
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionCentre for Research into Topical Drug Delivery and Toxicology
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.contributor.institutionNatural Product Chemistry and Drug Design
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=41649095370&partnerID=8YFLogxK
rioxxterms.versionVoR
rioxxterms.versionofrecordhttps://doi.org/10.1021/ci700282u
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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