Anisotropic dynamics of the JE-2147-HIV protease complex: drug resistance and thermodynamic binding mode examined in a 1.09 A structure.

@article{Reiling2002AnisotropicDO,
  title={Anisotropic dynamics of the JE-2147-HIV protease complex: drug resistance and thermodynamic binding mode examined in a 1.09 A structure.},
  author={K Kinkead Reiling and Nicholas F. Endres and Deborah S Dauber and Charles S. Craik and Robert Michael Stroud},
  journal={Biochemistry},
  year={2002},
  volume={41 14},
  pages={4582-94}
}
The structure of HIV protease (HIV Pr) bound to JE-2147 (also named AG1776 or KNI-764) is determined here to 1.09 A resolution. This highest-resolution structure for HIV Pr allows refinement of anisotropic displacement parameters (ADPs) for all atoms. Clustering based on the directional information in ADPs defines two sets of subdomains such that within each set, subdomains undergo similar anisotropic motion. These sets are (a) the core of monomer A grouped with both substrate-binding flaps and… CONTINUE READING