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Article

Disulfide exchange in domain 2 of CD4 is required for entry of HIV-1.

Nature immunology - 1 Aug 2002

Matthias Lisa J, Yam Patricia T W, Jiang Xing-Mai, Vandegraaff Nick, Li Peng, Poumbourios Pantelis, Donoghue Neil, Hogg Philip J

Abstract excerpt

CD4, a member of the immunoglobulin superfamily of receptors that mediates cell-cell interactions in the immune system, is the primary receptor for HIV-1. The extracellular portion of CD4 is a concatenation of four immunoglobulin-like domains, D1 to D4. The D1, D2 and D4 domains each contain a disulfide bond. We show here that the D2 disulfide bond is redox-active. The redox state of the thiols (disulfide versus...

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Identifiers

PMID: 12089508
DOI: 10.1038/ni815

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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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