1onq: Difference between revisions
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==Overview== | ==Overview== | ||
CD1 antigens bind a variety of self and foreign lipid and glycolipid | 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. | ||
==Disease== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Elsliger, M | [[Category: Elsliger, M A.]] | ||
[[Category: Teyton, L.]] | [[Category: Teyton, L.]] | ||
[[Category: Wilson, I | [[Category: Wilson, I A.]] | ||
[[Category: Zajonc, D | [[Category: Zajonc, D M.]] | ||
[[Category: FUC]] | [[Category: FUC]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
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[[Category: protein-glycolipid complex]] | [[Category: protein-glycolipid complex]] | ||
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Revision as of 15:19, 21 February 2008
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Crystal Structure of CD1a in Complex with a Sulfatide
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this StructureAbout this Structure
1ONQ is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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