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4pp8

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(New page: '''Unreleased structure''' The entry 4pp8 is ON HOLD Authors: Li, P., Strong, R.K. Description: Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D)
Current revision (07:22, 8 February 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4pp8 is ON HOLD
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==Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D==
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<StructureSection load='4pp8' size='340' side='right'caption='[[4pp8]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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Authors: Li, P., Strong, R.K.
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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>
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Description: Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4pp8" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[NK cell receptor|NK cell receptor]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Li P]]
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[[Category: Strong RK]]

Current revision

Crystal structure of murine NK cell ligand RAE-1 beta in complex with NKG2D

PDB ID 4pp8

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