Nature Immunology
2, 248 - 254 (2001)
doi:10.1038/85311
Crystal structure of the murine NK cell−activating receptor NKG2D at 1.95 ÅDennis W. Wolan1, Luc Teyton2, Markus G. Rudolph1, Brigitte Villmow3, Stefan Bauer3, Dirk H. Busch3
& Ian A. Wilson11
Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. 2
Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. 3
Institute of Medical Microbiology, Immunology and Hygiene, Technical University Munich, Trogerstrasse 9, 81675 Munich, Germany.
Correspondence should be addressed to Ian A. Wilson wilson@scripps.edu or Dirk H. Busch dirk.busch@lrz.tum.deNKG2D, a homodimeric lectin-like receptor, is a unique stimulatory molecule that is found on natural killer cells, T cells and activated macrophages. The natural ligands for murine NKG2D are distant major histocompatibility complex homologs, retinoic acid early transcript (Rae1) and H-60 minor histocompatibility antigen. The crystal structure of the extracellular region of murine NKG2D reveals close homology with other C-type lectin receptors such as CD94, Ly49A, rat MBP-A and CD69. However, the precise mode of dimeric assembly varies among these natural killer receptors, as well as their surface topography and electrostatic properties. The NKG2D structure provides the first structural insights into the role and ligand specificity of this stimulatory receptor in the innate and adaptive immune system.
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