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Article

Immunological evidence for interactions between the first, second, and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1.

Journal of virology - 1 Nov 1994

Moore J P, Willey R L, Lewis G K, Robinson J, Sodroski J

Abstract excerpt

We have used a combination of genetic and immunological techniques to explore how amino acid substitutions in the second conserved (C2) domain of gp120 from human immunodeficiency virus type 1 (HIV-1) affect the conformation of the protein. It was reported previously (R. L. Willey, E. K. Ross, A. J. Buckler-White, T. S. Theodore, and M. A. Martin. J. Viol. 63:3595-3600, 1989) that an asparagine-glutamine (N/Q)...

Topics

Amino Acid Sequence
CD4 Antigens
Conserved Sequence
HIV Envelope Protein gp120
Molecular Sequence Data
Mutation
Protein Conformation
Structure-Activity Relationship

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 7933065
DOI: 10.1128/JVI.68.11.6836-6847.1994
PMCID: PMC237119

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7933065-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Immunological evidence for interactions between the first, second, and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1.PMID 7933065Read ↗

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