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| | ==Antigen presenting molecule== | | ==Antigen presenting molecule== |
| - | <StructureSection load='5j1a' size='340' side='right' caption='[[5j1a]], [[Resolution|resolution]] 1.86Å' scene=''> | + | <StructureSection load='5j1a' size='340' side='right'caption='[[5j1a]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j1a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j1a]] is a 2 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=5J1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J1A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6F8:3-[(8Z,11Z)-PENTADECA-8,11-DIEN-1-YL]BENZENE-1,2-DIOL'>6F8</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]] 1.86Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), B2M, CDABP0092, HDCMA22P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6F8:3-[(8Z,11Z)-PENTADECA-8,11-DIEN-1-YL]BENZENE-1,2-DIOL'>6F8</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=5j1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j1a OCA], [http://pdbe.org/5j1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j1a RCSB], [http://www.ebi.ac.uk/pdbsum/5j1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j1a ProSAT]</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=5j1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j1a OCA], [https://pdbe.org/5j1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j1a RCSB], [https://www.ebi.ac.uk/pdbsum/5j1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j1a 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Beta-2 microglobulin|Beta-2 microglobulin]] | + | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] |
| | + | *[[CD1|CD1]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Marquez, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Nours, J Le]] | + | [[Category: Le Nours J]] |
| - | [[Category: Rossjohn, J]] | + | [[Category: Marquez E]] |
| - | [[Category: Winau, F]] | + | [[Category: Rossjohn J]] |
| - | [[Category: Yongqing, T]] | + | [[Category: Winau F]] |
| - | [[Category: Cd1 molecules immunity]] | + | [[Category: Yongqing T]] |
| - | [[Category: Immune system-inhibitor complex]]
| + | |
| Structural highlights
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
CD1a is a lipid-presenting molecule that is abundantly expressed on Langerhans cells. However, the in vivo role of CD1a has remained unclear, principally because CD1a is lacking in mice. Through the use of mice with transgenic expression of CD1a, we found that the plant-derived lipid urushiol triggered CD1a-dependent skin inflammation driven by CD4(+) helper T cells that produced the cytokines IL-17 and IL-22 (TH17 cells). Human subjects with poison-ivy dermatitis had a similar cytokine signature following CD1a-mediated recognition of urushiol. Among various urushiol congeners, we identified diunsaturated pentadecylcatechol (C15:2) as the dominant antigen for CD1a-restricted T cells. We determined the crystal structure of the CD1a-urushiol (C15:2) complex, demonstrating the molecular basis of urushiol interaction with the antigen-binding cleft of CD1a. In a mouse model and in patients with psoriasis, CD1a amplified inflammatory responses that were mediated by TH17 cells that reacted to self lipid antigens. Treatment with blocking antibodies to CD1a alleviated skin inflammation. Thus, we propose CD1a as a potential therapeutic target in inflammatory skin diseases.
CD1a on Langerhans cells controls inflammatory skin disease.,Kim JH, Hu Y, Yongqing T, Kim J, Hughes VA, Le Nours J, Marquez EA, Purcell AW, Wan Q, Sugita M, Rossjohn J, Winau F Nat Immunol. 2016 Oct;17(10):1159-66. doi: 10.1038/ni.3523. Epub 2016 Aug 22. PMID:27548435[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Kim JH, Hu Y, Yongqing T, Kim J, Hughes VA, Le Nours J, Marquez EA, Purcell AW, Wan Q, Sugita M, Rossjohn J, Winau F. CD1a on Langerhans cells controls inflammatory skin disease. Nat Immunol. 2016 Oct;17(10):1159-66. doi: 10.1038/ni.3523. Epub 2016 Aug 22. PMID:27548435 doi:http://dx.doi.org/10.1038/ni.3523
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