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[[Image:1jfm.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA==
|PDB= 1jfm |SIZE=350|CAPTION= <scene name='initialview01'>1jfm</scene>, resolution 2.85&Aring;
<StructureSection load='1jfm' size='340' side='right'caption='[[1jfm]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1jfm]] is a 5 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JFM FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
|GENE= RAE-1beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfm OCA], [https://pdbe.org/1jfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jfm RCSB], [https://www.ebi.ac.uk/pdbsum/1jfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jfm ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|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>
[https://www.uniprot.org/uniprot/RAE1B_MOUSE RAE1B_MOUSE] Acts as a ligand for NKG2D.<ref>PMID:10894171</ref>
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''CRYSTAL STRUCTURE OF MURINE NK CELL LIGAND RAE-1 BETA'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/1jfm_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jfm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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==
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<ref>PMID:11825567</ref>
1JFM is a [[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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/11825567 11825567]
</div>
<div class="pdbe-citations 1jfm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Li P]]
[[Category: Li, P.]]
[[Category: Strong RK]]
[[Category: Strong, R K.]]
[[Category: mhc-i platform]]
[[Category: murine nk cell ligand]]
[[Category: nkg2d]]
[[Category: rae-1 beta]]
 
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