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Article

Characterization of an active single polypeptide form of the human immunodeficiency virus type 1 protease.

The Journal of biological chemistry - 5 Oct 1990

DiIanni C L, Davis L J, Holloway M K, Herber W K, Darke P L, Kohl N E, Dixon R A

Abstract excerpt

The pepsin-like aspartyl proteases consist of a single polypeptide chain with topologically similar amino- and carboxyl-terminal domains, each of which contributes 1 aspartic acid residue to the active site. This structure has been proposed to have evolved by gene duplication and fusion from a di...

Topics

Amino Acid Sequence
Base Sequence
Binding Sites
Cloning, Molecular
Codon
Genes, Synthetic
Genes, Viral
HIV Protease
HIV-1
Kinetics
Macromolecular Substances
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Protein Conformation

Viral Structural Proteins

Source

Identifiers

PMID: 2211628

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2211628-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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