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1jfm

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|ACTIVITY=
|ACTIVITY=
|GENE= RAE-1beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= RAE-1beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfm OCA], [http://www.ebi.ac.uk/pdbsum/1jfm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jfm RCSB]</span>
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[[Category: rae-1 beta]]
[[Category: rae-1 beta]]
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Revision as of 18:33, 30 March 2008


PDB ID 1jfm

Drag the structure with the mouse to rotate
, resolution 2.85Å
Gene: RAE-1beta (Mus musculus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA


Overview

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.

About this Structure

1JFM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D., Li P, McDermott G, Strong RK, Immunity. 2002 Jan;16(1):77-86. PMID:11825567

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