1hyr
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The major histocompatibility complex (MHC) class I homolog, MICA, is a | + | 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== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Li, P.]] | [[Category: Li, P.]] | ||
| - | [[Category: Strong, R | + | [[Category: Strong, R K.]] |
[[Category: activating nk cell receptor]] | [[Category: activating nk cell receptor]] | ||
[[Category: c-type-lectin like]] | [[Category: c-type-lectin like]] | ||
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[[Category: nkg2d]] | [[Category: nkg2d]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:10 2008'' |
Revision as of 11:06, 21 February 2008
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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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