Role of Transmembrane Domain Interactions in the Assembly of Class II MHC Molecules

Evidence is presented that suggests a role for transmembrane domain interactions in the assembly of class II major histocompatibility complex (MHC) molecules. Mutations in the transmembrane domains of the class II MHC α or β chains resulted in proteins that did not generate complexes recognized by c...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1992-10, Vol.258 (5082), p.659-662
Main Authors: Cosson, Pierre, Bonifacino, Juan S.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies
Antigens
Biological and medical sciences
CD4 antigen
CD8 antigen
Cell Line
Cellular immunity
Cellular metabolism
Chimeras
clonal selection
Cloning, Molecular
COS cells
differentiation
DNA Mutational Analysis
Endoplasmic Reticulum - metabolism
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Glycine - metabolism
Histocompatibility antigens (hla, h-2 and other systems)
Histocompatibility Antigens Class II - biosynthesis
Histocompatibility Antigens Class II - chemistry
Histocompatibility Antigens Class II - genetics
lymphocytes T
Major histocompatibility complex
Mice
Microscopy
Molecular immunology
Molecular interactions
Molecular Sequence Data
Molecules
negative
Physiological aspects
Protein Conformation
Protein structure
Proteins
Receptors, Interleukin-2 - biosynthesis
Receptors, Interleukin-2 - chemistry
Receptors, Interleukin-2 - genetics
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Structure
T lymphocytes
thymocytes
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Description
Summary:Evidence is presented that suggests a role for transmembrane domain interactions in the assembly of class II major histocompatibility complex (MHC) molecules. Mutations in the transmembrane domains of the class II MHC α or β chains resulted in proteins that did not generate complexes recognized by conformation-dependent antibodies and that were largely retained in the endoplasmic reticulum. Insertion of the α and β transmembrane domains into other proteins allowed the chimeric proteins to assemble, suggesting a direct interaction of the α and β transmembrane domains. The interactions were mediated by a structural motif involving several glycine residues on the same face of a putative α helix.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1329208