Article
Investigating protein-ligand interactions with a mutant FKBP possessing a designed specificity pocket.
Journal of medicinal chemistry - 23 Mar 2000
Yang W, Rozamus L W, Narula S, Rollins C T, Yuan R, Andrade L J, Ram M K, Phillips T B, van Schravendijk M R, Dalgarno D, Clackson T, Holt D A
Abstract excerpt
Using structure-based design and protein mutagenesis we have remodeled the FKBP12 ligand binding site to include a sizable, hydrophobic specificity pocket. This mutant (F36V-FKBP) is capable of binding, with low or subnanomolar affinities, novel synthetic ligands possessing designed substituents that sterically prevent binding to the wild-type protein. Using binding and structural analysis of bumped compounds, we...
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