Role of Transmembrane Domain Interactions in the Assembly of Class II MHC Molecules
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- Pierre Cosson
- Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
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- Juan S. Bonifacino
- Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
説明
<jats:p>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.</jats:p>
収録刊行物
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- Science
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Science 258 (5082), 659-662, 1992-10-23
American Association for the Advancement of Science (AAAS)
