1jfm: Difference between revisions

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{{STRUCTURE_1jfm|  PDB=1jfm  |  SCENE=  }}  
{{STRUCTURE_1jfm|  PDB=1jfm  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA'''
===CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA===




==Overview==
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Induced by retinoic acid and implicated in playing a role in development, rodent RAE-1 proteins are ligands for the activating immunoreceptor NKG2D, widely expressed on natural killer cells, T cells, and macrophages. RAE-1 proteins (alpha, beta, gamma, and delta) are distant major histocompatibility complex (MHC) class I homologs, comprising isolated alpha1alpha2 platform domains. The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds. The loss of any remnant of a peptide binding groove was facilitated by the close approach of the groove-defining helices through a hydrophobic, leucine-rich interface. The RAE-1beta-murine NKG2D complex structure resembled the human NKG2D-MICA receptor-ligand complex and further demonstrated the promiscuity of the NKG2D ligand binding site.
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==About this Structure==
==About this Structure==
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[[Category: Nkg2d]]
[[Category: Nkg2d]]
[[Category: Rae-1 beta]]
[[Category: Rae-1 beta]]
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