1HYR

CRYSTAL STRUCTURE OF HUMAN MICA IN COMPLEX WITH NATURAL KILLER CELL RECEPTOR NKG2D

Summary for 1HYR

• Entry DOI: 10.2210/pdb1hyr/pdb
• Descriptor: NKG2-D TYPE II INTEGRAL MEMBRANE PROTEIN, MHC CLASS I CHAIN-RELATED PROTEIN A (3 entities in total)
• Functional Keywords: activating nk cell receptor, nkg2d, c-type-lectin like, mic-a, mhc-i, complex, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type II membrane protein: P26718
• Total number of polymer chains: 3
• Total formula weight: 63431.24

Authors

Li, P.,Strong, R.K. (deposition date: 2001-01-21, release date: 2001-05-23, Last modification date: 2024-10-09)

Primary citation

Li, P.,Morris, D.L.,Willcox, B.E.,Steinle, A.,Spies, T.,Strong, R.K.
Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA.
Nat.Immunol., 2:443-451, 2001

PubMed Abstract: 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 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.

PubMed: 11323699

Experimental method

X-RAY DIFFRACTION (2.7 Å)