Conformational changes induced in the MHC class I molecule by peptide and beta 2-microglobulin

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

J C Solheim1, J R Cook, T H Hansen

  • 1Department of Genetics, Washington University School of Medicine, St. Louis, Mo., USA.

Immunologic Research
|January 1, 1995
PubMed

Assembly of the class I MHC molecule is inextricably linked to the antigen presentation function of the class I molecule. Association of the class I MHC molecule with beta 2-microglobulin (beta 2m) is a prerequisite for association with the heterodimeric protein TAP, and once peptide is acquired, the class I molecule folds and begins its sojourn to the cell surface. To maintain its folded conformation, class I MHC requires peptide but not beta 2m, and the sequence of the peptide bound exercises a subtle influence on the structure of the class I molecule that is likely to be a factor in T cell receptor discrimination of MHC/peptide complexes.

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