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The acquisition of an optimal peptide ligand by MHC class I molecules is crucial for the generation of immunity to viruses and tumors. This process is orchestrated by a molecular machine known as the peptide loading complex (PLC) that consists of specialized and general ER-resident molecules. These proteins collaborate to ensure the loading of an optimal peptide ligand into the antigen binding cleft of class I molecules. The surprising diversity of peptides bound to MHC class I molecules and recapitulation of class I assembly in vitro have provided new insights into the molecular machinations of peptide loading. Coupled with the extraordinary polymorphism of class I molecules and their differential dependence on various components of the PLC for cell surface expression, a picture of peptide loading at the molecular level has recently emerged and will be discussed herein.

Original publication

DOI

10.1016/j.coi.2007.12.005

Type

Journal article

Journal

Current opinion in immunology

Publication Date

02/2008

Volume

20

Pages

75 - 81

Addresses

Department of Biochemistry and Molecular Biology, Bio21 Institute for Molecular Science and Biotechnology, University of Melbourne, Parkville, Victoria 3010, Australia.

Keywords

Endoplasmic Reticulum, Humans, Peptides, Histocompatibility Antigens Class I, Antigen Presentation, Polymorphism, Genetic