Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1

The crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A resolution. Large regions of the protease dimer, including the active site, have structural homology to t...

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Veröffentlicht in:	Nature (London) 1989-02, Vol.337 (6208), p.615-620
Hauptverfasser:	NAVIA, M. A, FITZGERALD, P. M. D, MCKEEVER, B. M, LEU, C.-T, HEIMBACH, J. C, HERBER, W. K, SIGAL, I. S, DARKE, P. L, SPRINGER, J. P
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV Aspartic Acid Endopeptidases aspartic proteinase Biological and medical sciences Endopeptidases - metabolism Enzymes Fundamental and applied biological sciences. Psychology HIV-1 - enzymology Human immunodeficiency virus 1 Macromolecular Substances Medical research Microbiology Models, Molecular Morphology, structure, chemical composition, physicochemical properties Protein Conformation proteinase Proteins Virology Viruses
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Beschreibung
Zusammenfassung:	The crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A resolution. Large regions of the protease dimer, including the active site, have structural homology to the family of microbial aspartyl proteases. The structure suggests a mechanism for the autoproteolytic release of protease and a role in the control of virus maturation.
ISSN:	0028-0836 1476-4687
DOI:	10.1038/337615a0