Putting together an MHC class I molecule

doi:10.1016/0952-7915(93)90076-5

Current Opinion in Immunology

Volume 5, Issue 1, February 1993, Pages 21-26

https://doi.org/10.1016/0952-7915(93)90076-5 Get rights and content

Abstract

Formation of MHC class I complexes involves proper folding of the subunits, their assembly and interaction with peptides. Several proteins contributing to this process have been described, but a number of questions remain, in particular those concerning early folding steps and interactions with peptide in the course of biosynthesis.

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Putting together an MHC class I molecule

Abstract

Assembly and Intracellular Transport of Major Histocompatibility Complex Molecules

Curr Opin Cell Biol

Intracellular Transport of HC Class 11 Molecules

Immunol Today

Invariant Chain Distinguishes Between the Exogenous and Endogenous Antigen Presentation Pathways

Nature

Segregation of MHC Class 11 Molecules from MHC Class I Molecules in the Golgi Complex for Transport to Lysosomal Compartments

Nature

Antigen Presentation: Structural Themes and Functional Variations

Immuno oday

Cell-free Translation of the mRNAs for the Heavy and Light Chains of HLA-A and HLA-B Antigens

Cellfree Synthesis and Membrane Insertion of Mouse H-2d Histocompatibility Antigen and β2-microglobulin

Cell

Association of Class I Major Histocompatibility Heavy and Light Chains Induced by Viral Peptides

Nature

Empty MHC Class I Molecules Come out in the Cold

Nature

Assembly of MHC Class I Molecules Analyzed in Vitro

Cell

Direct Binding of Peptide to Empty MHC Class I Molecules on Intact Cells and in Vitro

Cell

Peptide-induced Stabilization and Intracellular Localization of Empty HLA Class I Complexes

J Exp Med

Peptide-induced Conformational Change of the Class I Heavy Chain

Nature

How do Peptides Associate with MHC Class I Molecules?

Immunol Today

Cytotoxic T Lymphocytes Recognize a Reconstituted Class I Histocompatibility Antigen (HLAA2) as an Allogeneic Target Molecule?

Reconstitution by MHC, restricted Peptides of HLA-A2 Heavy Chain with β2-microglobulin, in Vitro

Nature

HLA-A2-peptide Complexes. Refolding and Crystallization of Molecules Expressed in Escherichia coli and Complexed with Single Antigenic Peptides

An HLA-A2/beta-2Microglobulin-Peptide Complex Assembled from Subunits Expressed Separately in Escherichia coli

Mol Immunol

Crystal Structure of the Major Histocompatibility Complex Class I H-2Kb Molecule Containing a Single Viral Peptide: Implications for Peptide Binding and T-cell Receptor Recognition

Protein Folding in the Cell

Nature

Role of ATP and Disulphide Bonds during Protein Folding in the Endoplasmic Reticulum

Nature

Manipulating Disulfide Formation and Protein Folding in the Endoplasmic Reticulum

EMBO J

Early Disulfide Bond Formation Prevents Heterotypic Aggregation of Membrane Proteins in a Cell-free Translation System

J Cell Biol

The Ligand-binding Conformation of Mr 46,000 Mannose 6-phosphate-specific Receptor

J Biol Chem

Independent and Synergistic Effects of Disulfide Bond Formation, [β2-microglobulin and Peptides on Class I MHC Folding and Assembly in an in Vitro translation system

J Immunol

Oxidized Redox State of ..Glutathione in the Endoplasmic Reticulum

Science

Participation of a Novel 88 kD Protein in the Biogenesis of Murine Class I Histocompatibility Molecules

J Cell Biol

Efficient Dissociation of the p88 Chaperone from Major Histocompatibility Complex Class I Molecules Requires Both β2-microglobulin and Peptide

J Exp Med

Endoplasmic Reticulum Resident Protein of 90 Kilodaltons Associates with the T- and B-cell Antigen Receptors and Major Histocompatibility Complex Antigens during Their Assembly

The p88 Molecular Chaperone is Identical to the Endoplasmic Reticulum Protein, Calnexin

J Biol Chem

Reconstitution by MHC, restricted Peptides of HLA-A2 Heavy Chain with β₂-microglobulin, in Vitro

Crystal Structure of the Major Histocompatibility Complex Class I H-2K^b Molecule Containing a Single Viral Peptide: Implications for Peptide Binding and T-cell Receptor Recognition

Efficient Dissociation of the p88 Chaperone from Major Histocompatibility Complex Class I Molecules Requires Both β₂-microglobulin and Peptide