Interaction Between CD8 and Major Histocompatibility Complex (MHC) Class I Mediated by Multiple Contact Surfaces That Include the Alpha 2 and Alpha 3 Domains of MHC Class I

Overview

Journal J Exp Med

Specialties Allergy & Immunology
General Medicine

Date 1995 Nov 1

PMID 7595198

Citations 18

Authors

J Sun

D J LEAHY

P B Kavathas

Affiliations

Soon will be listed here.

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 alpha 2 and alpha 3 domains of class I. Using a cell-cell adhesion assay, we identified three residues Q115, D122, and E128 in the alpha 2 domain of class I critical for interaction with CD8. The side chains of these residues point towards a cavity formed by the alpha 1/alpha 2 platform, the alpha 3 domain and beta 2-microglobulin (beta 2m) of class I. These residues were predicted to contact CD8 based on a bivalent model of interaction between one CD8 alpha/alpha homodimer and two MHC class I molecules. These results therefore provide support for the model.

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