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Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease

Wlodawer, Alexander and Miller, Maria and Jaskólski, Mariusz and Sathyanarayana, Bangalore K. and Baldwin, Eric and Weber, Irene T. and Selk, Linda M. and Clawson, Leigh and Schneider, Jens and Kent, Stephen B. H. (1989) Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science, 245 (4918). pp. 616-621. ISSN 0036-8075. https://resolver.caltech.edu/CaltechAUTHORS:20150128-103636013

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Abstract

The rational design of drugs that can inhibit the action of viral proteases depends on obtaining accurate structures of these enzymes. The crystal structure of chemically synthesized HIV-1 protease has been determined at 2.8 angstrom resolution (R factor of 0.184) with the use of a model based on the Rous sarcoma virus protease structure. In this enzymatically active protein, the cysteines were replaced by alpha-amino-n-butyric acid, a nongenetically coded amino acid. This structure, in which all 99 amino acids were located, differs in several important details from that reported previously by others. The interface between the identical subunits forming the active protease dimer is composed of four well-ordered β strands from both the amino and carboxyl termini and residues 86 to 94 have a helical conformation. The observed arrangement of the dimer interface suggests possible designs for dimerization inhibitors.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.2548279DOIArticle
http://www.sciencemag.org/content/245/4918/616PublisherArticle
http://www.jstor.org/stable/1704459JSTORArticle
Additional Information:© 1989 American Association for the Advancement of Science. 26 May 1989; Accepted 10 July 1989. We thank the Advanced Scientific Computing Laboratory, FCRF, for computer time on their CRAY X-MP. Sponsored in part by the National Cancer Institute, DHHS, under contract N01-CO-74101 with BRI, and in part by funds from the NSF Biological Instrumentation Division to S.B.H.K.
Funders:
Funding AgencyGrant Number
National Cancer InstituteN01-CO-74101
Department of Health and Human Services (DHHS)UNSPECIFIED
NSFUNSPECIFIED
Issue or Number:4918
Record Number:CaltechAUTHORS:20150128-103636013
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150128-103636013
Official Citation:Wlodawer, A., Miller, M., Jaskolski, M., Sathyanarayana, B., Baldwin, E., Weber, I., . . . Kent, S. (1989). Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science, 245(4918), 616-621. doi: 10.1126/science.2548279
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54183
Collection:CaltechAUTHORS
Deposited By: Joanne McCole
Deposited On:28 Jan 2015 20:08
Last Modified:03 Oct 2019 07:55

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