Please use this identifier to cite or link to this item: https://doi.org/10.1021/jm701190v
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dc.titleExploring inhibitor binding at the S′ subsites of cathepsin L
dc.contributor.authorChowdhury, S.F.
dc.contributor.authorJoseph, L.
dc.contributor.authorKumar, S.
dc.contributor.authorTulsidas, S.R.
dc.contributor.authorBhat, S.
dc.contributor.authorZiomek, E.
dc.contributor.authorMénard, R.
dc.contributor.authorSivaraman, J.
dc.contributor.authorPurisima, E.O.
dc.date.accessioned2014-10-27T08:28:00Z
dc.date.available2014-10-27T08:28:00Z
dc.date.issued2008-03-13
dc.identifier.citationChowdhury, S.F., Joseph, L., Kumar, S., Tulsidas, S.R., Bhat, S., Ziomek, E., Ménard, R., Sivaraman, J., Purisima, E.O. (2008-03-13). Exploring inhibitor binding at the S′ subsites of cathepsin L. Journal of Medicinal Chemistry 51 (5) : 1361-1368. ScholarBank@NUS Repository. https://doi.org/10.1021/jm701190v
dc.identifier.issn00222623
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100632
dc.description.abstractWe report a series of noncovalent, reversible inhibitors of cathepsin L that have been designed to explore additional binding interactions with the S′ subsites. The design was based on our previously reported crystal structure that suggested the possibility of engineering increased interactions with the S′ subsites (Chowdhury et al. J. Med. Chem. 2002, 45, 5321-5329). A representative of these new inhibitors has been co-crystallized with mature cathepsin L, and the structure has been solved and refined at 2.2 Å. The inhibitors described in this work extend farther into the S′ subsites of cathepsins than any inhibitors reported in the literature thus far. These interactions appear to make use of a S3′ subsite that can potentially be exploited for enhanced specificity and/or affinity. © 2008 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/jm701190v
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/jm701190v
dc.description.sourcetitleJournal of Medicinal Chemistry
dc.description.volume51
dc.description.issue5
dc.description.page1361-1368
dc.description.codenJMCMA
dc.identifier.isiut000253784900027
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