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Article

A mechanism by which binding of the broadly neutralizing antibody b12 unfolds the inner domain α1 helix in an engineered HIV-1 gp120.

Proteins - 1 Feb 2011

Emileh Ali, Abrams Cameron F

Abstract excerpt

Using all-atom simulations, we examine the role of the I109C/Q428C disulfide "stitch" in altering the conformational distribution of engineered HIV-1 gp120 core relevant for binding of the broadly neutralizing recombinant antibody b12. In particular, we propose that the I109C/Q428C stitch results...

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Share to Antibodies, Neutralizing
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Envelope Protein gp120

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Share to Protein Structure, Secondary

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Source

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Identifiers

PMID: 21117239
DOI: 10.1002/prot.22901
PMCID: PMC3059550

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21117239-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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