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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-02

AUTHORS

M A Navia, P M Fitzgerald, B M McKeever, C T Leu, J C Heimbach, W K Herber, I S Sigal, P L Darke, J P Springer

ABSTRACT

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. More... »

PAGES

615-620

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/337615a0

DOI

http://dx.doi.org/10.1038/337615a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037836841

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2645523


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