1H NMR structure and biological studies of the His23-->Cys mutant nucleocapsid protein of HIV-1 indicate that the conformation of the first zinc finger is critical for virus infectivity.

doi:10.1021/bi00205a006

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Article

1H NMR structure and biological studies of the His23-->Cys mutant nucleocapsid protein of HIV-1 indicate that the conformation of the first zinc finger is critical for virus infectivity.

Biochemistry - 4 Oct 1994

Déméné H, Dong C Z, Ottmann M, Rouyez M C, Jullian N, Morellet N, Mely Y, Darlix J L, Fournié-Zaluski M C, Saragosti S

Abstract excerpt

The nucleocapsid protein NCp7 of human immunodeficiency virus type 1 (HIV-1), which has key functions in the virus life cycle, possesses two zinc fingers of the CX2CX4HX4C type characterized by three successive loops containing a tetrahedrally coordinated zinc atom. The replacement of any cysteine by a serine in either finger has been shown to result in the production of noninfectious viruses, probably by...

Topics

Amino Acid Sequence
Capsid
Capsid Proteins
Cysteine
Gene Products, gag
HIV-1
Histidine
Humans
Magnetic Resonance Spectroscopy
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Protein Conformation

Structure-Activity Relationship

T-Lymphocytes, Regulatory

Transfection

Viral Proteins

Virulence

Source

Open in PubMed

Identifiers

PMID: 7918387
DOI: 10.1021/bi00205a006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7918387-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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1H NMR structure and biological studies of the His23-->Cys mutant nucleocapsid protein of HIV-1 indicate that the conformation of the first zinc finger is critical for virus infectivity.PMID 7918387Read ↗

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