1onq: Difference between revisions

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{{Seed}}
[[Image:1onq.png|left|200px]]


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==Crystal Structure of CD1a in Complex with a Sulfatide==
The line below this paragraph, containing "STRUCTURE_1onq", creates the "Structure Box" on the page.
<StructureSection load='1onq' size='340' side='right'caption='[[1onq]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1onq]] 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=1ONQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ONQ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SLF:SULFATE-3-D-GALACTOSYL-BETA-1-1-N-STEAROYL-D-SPHINGOSINE'>SLF</scene></td></tr>
{{STRUCTURE_1onq|  PDB=1onq  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1onq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1onq OCA], [https://pdbe.org/1onq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1onq RCSB], [https://www.ebi.ac.uk/pdbsum/1onq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1onq ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/on/1onq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1onq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs). Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket. The headgroup is anchored in the A'-F' junction and protrudes into the F' pocket for TCR recognition. Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.


===Crystal Structure of CD1a in Complex with a Sulfatide===
Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.,Zajonc DM, Elsliger MA, Teyton L, Wilson IA Nat Immunol. 2003 Aug;4(8):808-15. Epub 2003 Jun 29. PMID:12833155<ref>PMID:12833155</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1onq" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12833155}}, adds the Publication Abstract to the page
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12833155 is the PubMed ID number.
*[[CD1|CD1]]
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== References ==
{{ABSTRACT_PUBMED_12833155}}
<references/>
 
__TOC__
==Disease==
</StructureSection>
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]]
 
==About this Structure==
1ONQ is a [[Protein complex]] structure of sequences 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=1ONQ OCA].
 
==Reference==
Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A., Zajonc DM, Elsliger MA, Teyton L, Wilson IA, Nat Immunol. 2003 Aug;4(8):808-15. Epub 2003 Jun 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12833155 12833155]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Elsliger, M A.]]
[[Category: Elsliger MA]]
[[Category: Teyton, L.]]
[[Category: Teyton L]]
[[Category: Wilson, I A.]]
[[Category: Wilson IA]]
[[Category: Zajonc, D M.]]
[[Category: Zajonc DM]]
[[Category: Beta sheet platform]]
[[Category: Protein-glycolipid complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:04:34 2008''

Latest revision as of 03:20, 21 November 2024

Crystal Structure of CD1a in Complex with a SulfatideCrystal Structure of CD1a in Complex with a Sulfatide

Structural highlights

1onq 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 2.15Å
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs). Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket. The headgroup is anchored in the A'-F' junction and protrudes into the F' pocket for TCR recognition. Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.

Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.,Zajonc DM, Elsliger MA, Teyton L, Wilson IA Nat Immunol. 2003 Aug;4(8):808-15. Epub 2003 Jun 29. PMID:12833155[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. ↑ Zajonc DM, Elsliger MA, Teyton L, Wilson IA. Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. Nat Immunol. 2003 Aug;4(8):808-15. Epub 2003 Jun 29. PMID:12833155 doi:10.1038/ni948

1onq, resolution 2.15Å

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