Molecular machinations of the MHC-I peptide loading complex
Molecular machinations of the MHC-I peptide loading complex
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
antigen, cell, endoplasmic-reticulum, expression, t-cell recognition, tapasin, time, protein, surface expression, erp57, in-vitro, tap, alpha-2 domain, antigen presentation, binding, immunity, absence, tumors
75-81
Purcell, A.W.
13dd9d73-69db-439b-a546-b3f7f63bb4c5
Elliott, T.
16670fa8-c2f9-477a-91df-7c9e5b453e0e
2008
Purcell, A.W.
13dd9d73-69db-439b-a546-b3f7f63bb4c5
Elliott, T.
16670fa8-c2f9-477a-91df-7c9e5b453e0e
Purcell, A.W. and Elliott, T.
(2008)
Molecular machinations of the MHC-I peptide loading complex.
Current Opinion in Immunology, 20 (1), .
Abstract
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
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Published date: 2008
Keywords:
antigen, cell, endoplasmic-reticulum, expression, t-cell recognition, tapasin, time, protein, surface expression, erp57, in-vitro, tap, alpha-2 domain, antigen presentation, binding, immunity, absence, tumors
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Local EPrints ID: 62885
URI: http://eprints.soton.ac.uk/id/eprint/62885
ISSN: 0952-7915
PURE UUID: 82f93b6b-420a-4c60-8eb4-cfb629645867
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Date deposited: 10 Sep 2008
Last modified: 09 Jan 2022 03:05
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Author:
A.W. Purcell
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