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Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA

Li, Pingwei and Morris, Daniel L. and Willcox, Benjamin E. and Steinle, Alexander and Spies, Thomas and Strong, Roland K. (2001) Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA. Nature Immunology, 2 (5). pp. 443-451. ISSN 1529-2908. doi:10.1038/87757.

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The major histocompatibility complex (MHC) class I homolog, MICA, is a stress-inducible ligand for NKG2D, a C-type lectin−like activating immunoreceptor. The crystal structure of this ligand-receptor complex that we report here reveals an NKG2D homodimer bound to a MICA monomer in an interaction that is analogous to that seen in T cell receptor−MHC class I protein complexes. Similar surfaces on each NKG2D monomer interact with different surfaces on either the α1 or α2 domains of MICA. The binding interactions are large in area and highly complementary. The central section of the α2-domain helix, disordered in the structure of MICA alone, is ordered in the complex and forms part of the NKG2D interface. The extensive flexibility of the interdomain linker of MICA is shown by its altered conformation when crystallized alone or in complex with NKG2D.

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Additional Information:© 2001 Nature Publishing Group. Received 20 February 2001; Accepted 23 March 2001. We thank L. Hung, G. McDermott and T. Earnest (Advanced Light Source, Lawrence Berkeley National Laboratory) for assistance with data collection. Supported by National Institutes of Health grants AI42200 (to R. K. S.), CA18221 and AI30581 (to T. S.).
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Issue or Number:5
Record Number:CaltechAUTHORS:20150505-142515914
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57244
Deposited By: Jason Perez
Deposited On:06 May 2015 14:27
Last Modified:10 Nov 2021 21:10

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