| Literature DB >> 8627611 |
P S Dragovich1, J E Barker, J French, M Imbacuan, V J Kalish, C R Kissinger, D R Knighton, C T Lewis, E W Moomaw, H E Parge, L A Pelletier, T J Prins, R E Showalter, J H Tatlock, K D Tucker, J E Villafranca.
Abstract
The structure-based design and subsequent chemical synthesis of novel, urea-containing FKBP12 inhibitors are described. These compounds are shown to disrupt the cis-trans peptidylprolyl isomerase activity of FKBP12 with inhibition constants (Ki,app) approaching 0.10 microM. Analyses of several X-ray crystal structures of FKBP12-urea complexes demonstrate that the urea-containing inhibitors associate with FKBP12 in a manner that is similar to, but significantly different from, that observed for the natural product FK506.Entities:
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Year: 1996 PMID： 8627611 DOI： 10.1021/jm950798a
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446