Delineation of antigen contact residues on an MHC class II molecule

J. Peccoud; P. Dellabona; P. Allen; C. Benoist; D. Mathis

Delineation of antigen contact residues on an MHC class II molecule

J. Peccoud, P. Dellabona, P. Allen, C. Benoist, D. Mathis

Research output: Contribution to journal › Article › peer-review

Abstract

This report describes a detailed mutational analysis of a major histocompatibility complex class II moleculethe a chain of the A^k complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of A^k by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.

Original language	English
Pages (from-to)	4215-4223
Number of pages	9
Journal	EMBO Journal
Volume	9
Issue number	13
State	Published - 1990

Keywords

Antigen presentation
Major histocompatibility complex
Site-specific mutagenesis
T cell recognition

Cite this

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abstract = "This report describes a detailed mutational analysis of a major histocompatibility complex class II moleculethe a chain of the Ak complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of Ak by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.",

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AU - Peccoud, J.

AU - Dellabona, P.

AU - Allen, P.

AU - Benoist, C.

AU - Mathis, D.

PY - 1990

Y1 - 1990

N2 - This report describes a detailed mutational analysis of a major histocompatibility complex class II moleculethe a chain of the Ak complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of Ak by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.

AB - This report describes a detailed mutational analysis of a major histocompatibility complex class II moleculethe a chain of the Ak complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of Ak by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.

KW - Antigen presentation

KW - Major histocompatibility complex

KW - Site-specific mutagenesis

KW - T cell recognition

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M3 - Article

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AN - SCOPUS:0025597053

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VL - 9

SP - 4215

EP - 4223

JO - EMBO Journal

JF - EMBO Journal

IS - 13

ER -

Delineation of antigen contact residues on an MHC class II molecule

Abstract

Keywords

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