1jfm
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(New page: 200px<br /><applet load="1jfm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jfm, resolution 2.85Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 16:04, 20 November 2007
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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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