Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.

doi:10.1128/JVI.68.1.240-250.1994

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Article

Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.

Journal of virology - 1 Jan 1994

Zybarth G, Kräusslich H G, Partin K, Carter C

Abstract excerpt

The mature human immunodeficiency virus type 1 proteinase (PR; 11 kDa) can cleave all interdomain junctions in the Gag and Gag-Pol polyprotein precursors. To determine the activity of the enzyme in its precursor form, we blocked release of mature PR from a truncated Gag-Pol polyprotein by introdu...

Topics

Amino Acid Sequence
Animals
Cell Line
Escherichia coli
Frameshift Mutation
Fusion Proteins, gag-pol
Gene Products, gag
HIV Protease
HIV-1
Molecular Sequence Data
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Oligopeptides

Protein Precursors

Protein Processing, Post-Translational

Recombinant Proteins

Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 8254734
DOI: 10.1128/JVI.68.1.240-250.1994
PMCID: PMC236283

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8254734-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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