1HQ8

CRYSTAL STRUCTURE OF THE MURINE NK CELL-ACTIVATING RECEPTOR NKG2D AT 1.95 A

Summary for 1HQ8

• Entry DOI: 10.2210/pdb1hq8/pdb
• Descriptor: NKG2-D (2 entities in total)
• Functional Keywords: homodimer, cis-proline, apoptosis
• Biological source: Mus musculus (house mouse)
• Cellular location: Membrane; Single-pass type II membrane protein (By similarity): O54709
• Total number of polymer chains: 1
• Total formula weight: 14114.84

Authors

Wolan, D.W.,Teyton, L.,Rudolph, M.G.,Villmow, B.,Bauer, S.,Busch, D.H.,Wilson, I.A. (deposition date: 2000-12-14, release date: 2001-03-07, Last modification date: 2024-10-16)

Primary citation

Wolan, D.W.,Teyton, L.,Rudolph, M.G.,Villmow, B.,Bauer, S.,Busch, D.H.,Wilson, I.A.
Crystal structure of the murine NK cell-activating receptor NKG2D at 1.95 A.
Nat.Immunol., 2:248-254, 2001

PubMed Abstract: NKG2D, 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.

PubMed: 11224525
DOI: 10.1038/85311

Experimental method

X-RAY DIFFRACTION (1.95 Å)