4x6c: Difference between revisions

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==Immune complex==
 
<StructureSection load='4x6c' size='340' side='right' caption='[[4x6c]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
==CD1a ternary complex with lysophosphatidylcholine and BK6 TCR==
<StructureSection load='4x6c' size='340' side='right'caption='[[4x6c]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4x6c]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X6C FirstGlance]. <br>
<table><tr><td colspan='2'>[[4x6c]] is a 8 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=4X6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X6C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=42H:(4R,7R,18Z)-4,7-DIHYDROXY-N,N,N-TRIMETHYL-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-18-EN-1-AMINIUM+4-OXIDE'>42H</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x6d|4x6d]], [[4x6b|4x6b]], [[4x6e|4x6e]], [[4x6f|4x6f]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=42H:(4R,7R,18Z)-4,7-DIHYDROXY-N,N,N-TRIMETHYL-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-18-EN-1-AMINIUM+4-OXIDE'>42H</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x6c RCSB], [http://www.ebi.ac.uk/pdbsum/4x6c PDBsum]</span></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=4x6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6c OCA], [https://pdbe.org/4x6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x6c RCSB], [https://www.ebi.ac.uk/pdbsum/4x6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6c ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[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> 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CD1A_HUMAN CD1A_HUMAN]] Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.<ref>PMID:11231314</ref> <ref>PMID:16272286</ref> <ref>PMID:18178838</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.  
[https://www.uniprot.org/uniprot/CD1A_HUMAN CD1A_HUMAN] Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.<ref>PMID:11231314</ref> <ref>PMID:16272286</ref> <ref>PMID:18178838</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A central paradigm in alphabeta T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the alphabeta T cell antigen receptor (TCR). CD1a presents a broad repertoire of lipid-based antigens. We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding. The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands. Nonpermissive ligands indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone. The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby alphabeta T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
 
alphabeta T cell antigen receptor recognition of CD1a presenting self lipid ligands.,Birkinshaw RW, Pellicci DG, Cheng TY, Keller AN, Sandoval-Romero M, Gras S, de Jong A, Uldrich AP, Moody DB, Godfrey DI, Rossjohn J Nat Immunol. 2015 Mar;16(3):258-266. doi: 10.1038/ni.3098. Epub 2015 Feb 2. PMID:25642819<ref>PMID:25642819</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4x6c" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[CD1|CD1]]
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Birkinshaw, R W]]
[[Category: Homo sapiens]]
[[Category: Rossjohn, J]]
[[Category: Large Structures]]
[[Category: Cd1a]]
[[Category: Birkinshaw RW]]
[[Category: Immune complex]]
[[Category: Rossjohn J]]
[[Category: Immune system]]
[[Category: Lipid antigen]]
[[Category: Tcr]]

Latest revision as of 10:41, 27 September 2023

CD1a ternary complex with lysophosphatidylcholine and BK6 TCRCD1a ternary complex with lysophosphatidylcholine and BK6 TCR

Structural highlights

4x6c is a 8 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 2.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CD1A_HUMAN Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.[1] [2] [3]

Publication Abstract from PubMed

A central paradigm in alphabeta T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the alphabeta T cell antigen receptor (TCR). CD1a presents a broad repertoire of lipid-based antigens. We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding. The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands. Nonpermissive ligands indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone. The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby alphabeta T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.

alphabeta T cell antigen receptor recognition of CD1a presenting self lipid ligands.,Birkinshaw RW, Pellicci DG, Cheng TY, Keller AN, Sandoval-Romero M, Gras S, de Jong A, Uldrich AP, Moody DB, Godfrey DI, Rossjohn J Nat Immunol. 2015 Mar;16(3):258-266. doi: 10.1038/ni.3098. Epub 2015 Feb 2. PMID:25642819[4]

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

See Also

References

  1. ↑ Salamero J, Bausinger H, Mommaas AM, Lipsker D, Proamer F, Cazenave JP, Goud B, de la Salle H, Hanau D. CD1a molecules traffic through the early recycling endosomal pathway in human Langerhans cells. J Invest Dermatol. 2001 Mar;116(3):401-8. PMID:11231314 doi:1264
  2. ↑ Vincent MS, Xiong X, Grant EP, Peng W, Brenner MB. CD1a-, b-, and c-restricted TCRs recognize both self and foreign antigens. J Immunol. 2005 Nov 15;175(10):6344-51. PMID:16272286
  3. ↑ Sloma I, Zilber MT, Vasselon T, Setterblad N, Cavallari M, Mori L, De Libero G, Charron D, Mooney N, Gelin C. Regulation of CD1a surface expression and antigen presentation by invariant chain and lipid rafts. J Immunol. 2008 Jan 15;180(2):980-7. PMID:18178838
  4. ↑ Birkinshaw RW, Pellicci DG, Cheng TY, Keller AN, Sandoval-Romero M, Gras S, de Jong A, Uldrich AP, Moody DB, Godfrey DI, Rossjohn J. alphabeta T cell antigen receptor recognition of CD1a presenting self lipid ligands. Nat Immunol. 2015 Mar;16(3):258-266. doi: 10.1038/ni.3098. Epub 2015 Feb 2. PMID:25642819 doi:http://dx.doi.org/10.1038/ni.3098

4x6c, resolution 2.80Å

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