Journal article
The Heterodimeric Assembly of the CD94-NKG2 Receptor Family and Implications for Human Leukocyte Antigen-E Recognition
LC Sullivan, CS Clements, T Beddoe, D Johnson, HL Hoare, J Lin, T Huyton, EJ Hopkins, HH Reid, MCJ Wilce, J Kabat, F Borrego, JE Coligan, J Rossjohn, AG Brooks
Immunity | Published : 2007
Abstract
The CD94-NKG2 receptor family that regulates NK and T cells is unique among the lectin-like receptors encoded within the natural killer cell complex. The function of the CD94-NKG2 receptors is dictated by the pairing of the invariant CD94 polypeptide with specific NKG2 isoforms to form a family of functionally distinct heterodimeric receptors. However, the structural basis for this selective pairing and how they interact with their ligand, HLA-E, is unknown. We describe the 2.5 Å resolution crystal structure of CD94-NKG2A in which the mode of dimerization contrasts with that of other homodimeric NK receptors. Despite structural homology between the CD94 and NKG2A subunits, the dimer interfac..
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Awarded by National Institute of Allergy and Infectious Diseases