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Article

Functional evolution of the HIV-1 envelope glycoprotein 120 association site of glycoprotein 41.

The Journal of biological chemistry - 24 Oct 2003

Poumbourios Pantelis, Maerz Anne L, Drummer Heidi E

Abstract excerpt

Protein-protein interaction surfaces can exhibit structural plasticity, a mechanism whereby an interface adapts to mutations as binding partners coevolve. The HIV-1 envelope glycoprotein gp120-gp41 complex, which is responsible for receptor attachment and membrane fusion, represents an extreme ex...

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Identifiers

PMID: 12923196
DOI: 10.1074/jbc.M305223200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12923196-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Functional evolution of the HIV-1 envelope glycoprotein 120 association site of glycoprotein 41.PMID 12923196Read ↗

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