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• W2098432967 abstract "Many activating immunoreceptors are protein complexes in which ligand recognition and signaling functions are provided by separate modules. Wucherpfennig and co-workers report the nuclear magnetic resonance structure of the heterotrimeric DAP12-NKG2C receptor. Many receptors that activate cells of the immune system are multisubunit membrane protein complexes in which ligand recognition and signaling functions are contributed by separate protein modules. Receptors and signaling subunits assemble through contacts among basic and acidic residues in their transmembrane domains to form the functional complexes. Here we report the nuclear magnetic resonance (NMR) structure of the membrane-embedded, heterotrimeric assembly formed by association of the DAP12 signaling module with the natural killer (NK) cell–activating receptor NKG2C. The main intramembrane contact site is formed by a complex electrostatic network involving five hydrophilic transmembrane residues. Functional mutagenesis demonstrated that similar polar intramembrane motifs are also important for assembly of the NK cell–activating NKG2D-DAP10 complex and the T cell antigen receptor (TCR)–invariant signaling protein CD3 complex. This structural motif therefore lies at the core of the molecular organization of many activating immunoreceptors." @default.
• W2098432967 created "2016-06-24" @default.
• W2098432967 creator A5030377405 @default.
• W2098432967 creator A5030650949 @default.
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• W2098432967 date "2010-10-03" @default.
• W2098432967 modified "2023-10-15" @default.
• W2098432967 title "The structural basis for intramembrane assembly of an activating immunoreceptor complex" @default.
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• W2098432967 doi "https://doi.org/10.1038/ni.1943" @default.
• W2098432967 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3215083" @default.
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