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Article

Structural basis for HIV-1 neutralization by a gp41 fusion intermediate-directed antibody.

Nature structural & molecular biology - 1 Aug 2006

Luftig Micah A, Mattu Marco, Di Giovine Paolo, Geleziunas Romas, Hrin Renee, Barbato Gaetano, Bianchi Elisabetta, Miller Michael D, Pessi Antonello, Carfí Andrea

Abstract excerpt

Elicitation of potent and broadly neutralizing antibodies is an important goal in designing an effective human immunodeficiency virus-1 (HIV-1) vaccine. The HIV-1 gp41 inner-core trimer represents a functionally and structurally conserved target for therapeutics. Here we report the 2.0-A-resolution crystal structure of the complex between the antigen-binding fragment of D5, an HIV-1 cross-neutralizing antibody,...

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Share to Antibodies, Monoclonal
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HIV Envelope Protein gp41

Share to Hydrophobic and Hydrophilic Interactions

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Source

Identifiers

PMID: 16862157
DOI: 10.1038/nsmb1127

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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