Investigating protein-ligand interactions with a mutant FKBP possessing a designed specificity pocket

…, MR van Schravendijk, D Dalgarno…

文献索引：Yang, Wu; Rozamus, Leonard W.; Narula, Surinder; Rollins, Carl T.; Yuan, Ruth; Andrade, Lawrence J.; Ram, Mary K.; Phillips, Thomas B.; Van Schravendijk, Marie Rose; Dalgarno, David; Clackson, Tim; Holt, Dennis A. Journal of Medicinal Chemistry, 2000 , vol. 43, # 6 p. 1135 - 1142

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被引用次数: 66

摘要

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 show here that the ...