3HVP

CONSERVED FOLDING IN RETROVIRAL PROTEASES. CRYSTAL STRUCTURE OF A SYNTHETIC HIV-1 PROTEASE

Summary for 3HVP

• Entry DOI: 10.2210/pdb3hvp/pdb
• Descriptor: UNLIGANDED HIV-1 PROTEASE (1 entity in total)
• Functional Keywords: hydrolase(acid proteinase)
• Biological source: Human immunodeficiency virus 1
• Cellular location: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P03369
• Total number of polymer chains: 1
• Total formula weight: 10764.64

Authors

Wlodawer, A.,Jaskolski, M.,Miller, M. (deposition date: 1989-08-08, release date: 1989-10-15, Last modification date: 2017-11-29)

Primary citation

Wlodawer, A.,Miller, M.,Jaskolski, M.,Sathyanarayana, B.K.,Baldwin, E.,Weber, I.T.,Selk, L.M.,Clawson, L.,Schneider, J.,Kent, S.B.
Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease.
Science, 245:616-621, 1989

PubMed 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 beta 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.

PubMed: 2548279

Experimental method

X-RAY DIFFRACTION (2.8 Å)