4pp8: Difference between revisions
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==Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D== | |||
<StructureSection load='4pp8' size='340' side='right'caption='[[4pp8]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pp8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jsk 1jsk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PP8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pp8 OCA], [https://pdbe.org/4pp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pp8 RCSB], [https://www.ebi.ac.uk/pdbsum/4pp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pp8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NKG2D_MOUSE NKG2D_MOUSE] Receptor for RAET1A, RAET1B, RAET1C, RAET1D, RAET1E, H60 and MULT1. Involved in the immune surveillance exerted by T and B lymphocytes.<ref>PMID:12370332</ref> | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4pp8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[NK cell receptor|NK cell receptor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Li P]] | |||
[[Category: Strong RK]] | |||