1jfm: Difference between revisions
New page: left|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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[[Image:1jfm.jpg|left|200px]]<br /><applet load="1jfm" size=" | [[Image:1jfm.jpg|left|200px]]<br /><applet load="1jfm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jfm, resolution 2.85Å" /> | caption="1jfm, resolution 2.85Å" /> | ||
'''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA'''<br /> | '''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA'''<br /> | ||
==Overview== | ==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 | 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== | ==About this Structure== | ||
1JFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1JFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Li, P.]] | [[Category: Li, P.]] | ||
[[Category: Strong, R | [[Category: Strong, R K.]] | ||
[[Category: mhc-i platform]] | [[Category: mhc-i platform]] | ||
[[Category: murine nk cell ligand]] | [[Category: murine nk cell ligand]] | ||
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[[Category: rae-1 beta]] | [[Category: rae-1 beta]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:06 2008'' | ||
Revision as of 14:22, 21 February 2008
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CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA
OverviewOverview
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 StructureAbout this Structure
1JFM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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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