1jfm

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{{Seed}}
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{{STRUCTURE_1jfm| PDB=1jfm | SCENE= }}
{{STRUCTURE_1jfm| PDB=1jfm | SCENE= }}
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'''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA'''
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===CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA===
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==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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The line below this paragraph, {{ABSTRACT_PUBMED_11825567}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11825567 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11825567}}
==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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:09:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:10:30 2008''

Revision as of 17:10, 1 July 2008

Image:1jfm.png

Template:STRUCTURE 1jfm

CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA

Template:ABSTRACT PUBMED 11825567

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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