Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution.

@article{Miller1989StructureOC,
  title={Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution.},
  author={Maria Miller and Jay Schneider and Bangalore K Sathyanarayana and Margit T{\'o}th and Garland R. Marshall and Lora Clawson and Linda M. Selk and Stephen B. H. Kent and Alexander Wlodawer},
  journal={Science},
  year={1989},
  volume={246 4934},
  pages={1149-52}
}
The structure of a complex between a peptide inhibitor with the sequence N-acetyl-Thr-Ile-Nle-psi[CH2-NH]-Nle-Gln-Arg.amide (Nle, norleucine) with chemically synthesized HIV-1 (human immunodeficiency virus 1) protease was determined at 2.3 A resolution (R factor of 0.176). Despite the symmetric nature of the unliganded enzyme, the asymmetric inhibitor lies in a single orientation and makes extensive interactions at the interface between the two subunits of the homodimeric protein. Compared with… CONTINUE READING