Approaches to solving the rigid receptor problem by identifying a minimal set of flexible residues during ligand docking.
Anderson, A.C., O'Neil, R.H., Surti, T.S., Stroud, R.M.(2001) Chem Biol 8: 445-457
- PubMed: 11358692 
- DOI: https://doi.org/10.1016/s1074-5521(01)00023-0
- Primary Citation of Related Structures:  
1F28 - PubMed Abstract: 
Using fixed receptor sites derived from high-resolution crystal structures in structure-based drug design does not properly account for ligand-induced enzyme conformational change and imparts a bias into the discovery and design of novel ligands. We sought to facilitate the design of improved drug leads by defining residues most likely to change conformation, and then defining a minimal manifold of possible conformations of a target site for drug design based on a small number of identified flexible residues.
Organizational Affiliation: 
Department of Biochemistry and Biophysics, University of California at San Francisco, Box 0448, 94143-0448, USA. amy.c.anderson@dartmouth.edu