Journal article

The structural basis for intramembrane assembly of an activating immunoreceptor complex

Matthew E Call, Kai W Wucherpfennig, James J Chou

Nature Immunology | NATURE PUBLISHING GROUP | Published : 2010

Abstract

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 ..

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University of Melbourne Researchers

Grants

Awarded by US National Institutes of Health


Awarded by NATIONAL HEART, LUNG, AND BLOOD INSTITUTE


Awarded by NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES


Awarded by NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING


Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES


Funding Acknowledgements

We thank S.C. Blacklow (Harvard Medical School) for pMM-LR6 vector; M.J. Call and members of the Chou lab for reading the manuscript and discussions; and J. Pyrdol for assistance with initial construct design and expression trials. Supported by the Helen Hay Whitney Foundation (M.E.C.), the Charles A. King Trust (M.E.C.) and the US National Institutes of Health (R01AI054520 to K.W.W., R01HL084329 to J.J.C. and EB002026 to the Center for Magnetic Resonance at the Massachusetts Institute of Technology, where NMR data were collected).