Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the α2 and α3 domains of MHC class I

Jiaren Sun, Daniel J. Leahy, Paula B. Kavathas

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

The cell surface glycoprotein CD8 functions as a coreceptor with the TCR on cytotoxic T lymphocytes. Mutational analysis of the binding site of CD8 for MHC class I predicted that distinct surfaces of CD8 would interact with both the α2 and α3 domains of class I. Using a cell-cell adhesion assay, we identified three residues Q115, D122, and E128 in the α2 domain of class I critical for interaction with CD8. The side chains of these residues point towards a cavity formed by the α1/α2 platform, the α3 domain and β- microglobulin (β2m) of class I. These residues were predicted to contact CD8 based on a bivalent model of interaction between one CD8α/α homodimer and two MHC class I molecules. These results therefore provide support for the model.

Original languageEnglish (US)
Pages (from-to)1275-1280
Number of pages6
JournalJournal of Experimental Medicine
Volume182
Issue number5
DOIs
StatePublished - Nov 1 1995
Externally publishedYes

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Major Histocompatibility Complex
Membrane Glycoproteins
Cytotoxic T-Lymphocytes
Cell Adhesion
Binding Sites

ASJC Scopus subject areas

  • Immunology

Cite this

Interaction between CD8 and major histocompatibility complex (MHC) class I mediated by multiple contact surfaces that include the α2 and α3 domains of MHC class I. / Sun, Jiaren; Leahy, Daniel J.; Kavathas, Paula B.

In: Journal of Experimental Medicine, Vol. 182, No. 5, 01.11.1995, p. 1275-1280.

Research output: Contribution to journalArticle

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