1hyr
CRYSTAL STRUCTURE OF HUMAN MICA IN COMPLEX WITH NATURAL KILLER CELL RECEPTOR NKG2DCRYSTAL STRUCTURE OF HUMAN MICA IN COMPLEX WITH NATURAL KILLER CELL RECEPTOR NKG2D
Structural highlights
FunctionNKG2D_HUMAN Receptor for MICA, MICB, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4. Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. Involved in the immune surveillance exerted by T- and B-lymphocytes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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 alpha1 or alpha2 domains of MICA. The binding interactions are large in area and highly complementary. The central section of the alpha2-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. Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA.,Li P, Morris DL, Willcox BE, Steinle A, Spies T, Strong RK Nat Immunol. 2001 May;2(5):443-51. PMID:11323699[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||