A. Wlodawer, M. Miller, M. Jaskolski, B.K. Sathyanarayana, et al., "Conserved folding in retroviral protease: crystal structure of a synthetic HIV-1 protease," Science, 245, 616-21, 11 August 1989.
Alexander Wlodawer (Frederick Cancer Research Facility, National Cancer Institute, NIH, Frederick, Md.): "The protease is the only enzyme encoded by the human immunodeficiency virus (HIV) for which the three-dimensional structure has been elucidated by X-ray crystallography. The knowledge of the structure of an enzyme is invaluable for the rational design of new drugs that might work as inhibitors. The HIV protease offers a clear target for designing drugs that might provide new therapeutic approaches to the treatment of AIDS.
"This paper followed by a few months our report on the structure of a related protease from Rous sarcoma virus [M. Miller, et al., Nature, 337:576-9, 1989] and our prediction of the structure of HIV protease [I. Weber, et al., Science, 243:928-31, 1989]. ...
