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Biochem Biophys Res Commun. 1989 Oct 16;164(1):30-8.

Substitution mutations of the highly conserved arginine 87 of HIV-1 protease result in loss of proteolytic activity.

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  • 1Division of Cancer Biology and Diagnosis, National Cancer Institute, Bethesda, MD 20892.

Abstract

The 297bp gene coding for the HIV-1 protease was chemically synthesized and expressed in E. coli. Single amino acid substitutions (Arg 87 - greater than Lys; Arg 87 - greater than Glu) were introduced in the C-terminally located conserved region GlyArgAsn of the protease gene in the wild-type clone. The products of the mutant and the wild-type clones were expressed at approximately similar levels at 30 minutes of induction but the mutant protease proteins accumulated as a function of time of induction unlike the wild-type protease which declined after 60 minutes. The mutants were completely devoid of proteolytic activity as determined in assays employing as substrates a synthetic nonapeptide and a gag related recombinant polyprotein.

PMID:
2679552
[PubMed - indexed for MEDLINE]
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