Exploring inhibitor binding at the S' subsites of cathepsin L

DOIResolve DOI: http://doi.org/10.1021/jm701190v
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TypeArticle
Volume51
Issue5
Pages13611368; # of pages: 8
SubjectBiotechnology; cathepsin L; Cathepsins; crystal structure; inhibitors; pha
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 A. 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
Publication date
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number49552
NPARC number3540211
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Record identifier613f0b21-4988-46cb-ba1a-ca62095f6cba
Record created2009-03-01
Record modified2016-05-09
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