1hyr
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(New page: 200px<br /> <applet load="1hyr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hyr, resolution 2.70Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:17, 12 November 2007
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CRYSTAL STRUCTURE OF HUMAN MICA IN COMPLEX WITH NATURAL KILLER CELL RECEPTOR NKG2D
Overview
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.
About this Structure
1HYR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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