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{{STRUCTURE_4lhu|  PDB=4lhu  |  SCENE=  }}
===Crystal Structure of 9C2 TCR bound to CD1d===
{{ABSTRACT_PUBMED_24076636}}


==Disease==
==Crystal Structure of 9C2 TCR bound to CD1d==
[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref>   Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
<StructureSection load='4lhu' size='340' side='right'caption='[[4lhu]], [[Resolution|resolution]] 2.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lhu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LHU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.87&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=JLS:(15Z)-N-[(2S,3S,4R)-1-(ALPHA-D-GALACTOPYRANOSYLOXY)-3,4-DIHYDROXYOCTADECAN-2-YL]TETRACOS-15-ENAMIDE'>JLS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4lhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lhu OCA], [https://pdbe.org/4lhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lhu RCSB], [https://www.ebi.ac.uk/pdbsum/4lhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lhu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD1D_HUMAN CD1D_HUMAN] Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.<ref>PMID:17475845</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The T cell repertoire comprises alphabeta and gammadelta T cell lineages. Although it is established how alphabeta T cell antigen receptors (TCRs) interact with antigen presented by antigen-presenting molecules, this is unknown for gammadelta TCRs. We describe a population of human Vdelta1+ gammadelta T cells that exhibit autoreactivity to CD1d and provide a molecular basis for how a gammadelta TCR binds CD1d-alpha-galactosylceramide (alpha-GalCer). The gammadelta TCR docked orthogonally, over the A' pocket of CD1d, in which the Vdelta1-chain, and in particular the germ line-encoded CDR1delta loop, dominated interactions with CD1d. The TCR gamma-chain sat peripherally to the interface, with the CDR3gamma loop representing the principal determinant for alpha-GalCer specificity. Accordingly, we provide insight into how a gammadelta TCR binds specifically to a lipid-loaded antigen-presenting molecule.


==Function==
CD1d-lipid antigen recognition by the gammadelta TCR.,Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI Nat Immunol. 2013 Sep 29. doi: 10.1038/ni.2713. PMID:24076636<ref>PMID:24076636</ref>
[[http://www.uniprot.org/uniprot/CD1D_HUMAN CD1D_HUMAN]] Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.<ref>PMID:17475845</ref> [[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4lhu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LHU OCA].
</div>
<div class="pdbe-citations 4lhu" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
<ref group="xtra">PMID:024076636</ref><references group="xtra"/><references/>
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[CD1|CD1]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Godfrey, D I.]]
[[Category: Large Structures]]
[[Category: Gras, S.]]
[[Category: Godfrey DI]]
[[Category: Nours, J Le.]]
[[Category: Gras S]]
[[Category: Pellicci, D G.]]
[[Category: Le Nours J]]
[[Category: Rossjohn, J.]]
[[Category: Pellicci DG]]
[[Category: Uldrich, A P.]]
[[Category: Rossjohn J]]
[[Category: Cd1d]]
[[Category: Uldrich AP]]
[[Category: Gammadelta tcr]]
[[Category: Immune system]]
[[Category: Lipid recognition]]
[[Category: Nkt cell]]
[[Category: Pbs-44]]

Latest revision as of 19:19, 20 September 2023

Crystal Structure of 9C2 TCR bound to CD1dCrystal Structure of 9C2 TCR bound to CD1d

Structural highlights

4lhu is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.87Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CD1D_HUMAN Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.[1]

Publication Abstract from PubMed

The T cell repertoire comprises alphabeta and gammadelta T cell lineages. Although it is established how alphabeta T cell antigen receptors (TCRs) interact with antigen presented by antigen-presenting molecules, this is unknown for gammadelta TCRs. We describe a population of human Vdelta1+ gammadelta T cells that exhibit autoreactivity to CD1d and provide a molecular basis for how a gammadelta TCR binds CD1d-alpha-galactosylceramide (alpha-GalCer). The gammadelta TCR docked orthogonally, over the A' pocket of CD1d, in which the Vdelta1-chain, and in particular the germ line-encoded CDR1delta loop, dominated interactions with CD1d. The TCR gamma-chain sat peripherally to the interface, with the CDR3gamma loop representing the principal determinant for alpha-GalCer specificity. Accordingly, we provide insight into how a gammadelta TCR binds specifically to a lipid-loaded antigen-presenting molecule.

CD1d-lipid antigen recognition by the gammadelta TCR.,Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI Nat Immunol. 2013 Sep 29. doi: 10.1038/ni.2713. PMID:24076636[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Chen X, Wang X, Keaton JM, Reddington F, Illarionov PA, Besra GS, Gumperz JE. Distinct endosomal trafficking requirements for presentation of autoantigens and exogenous lipids by human CD1d molecules. J Immunol. 2007 May 15;178(10):6181-90. PMID:17475845
  2. ↑ Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI. CD1d-lipid antigen recognition by the gammadelta TCR. Nat Immunol. 2013 Sep 29. doi: 10.1038/ni.2713. PMID:24076636 doi:http://dx.doi.org/10.1038/ni.2713

4lhu, resolution 2.87Å

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