1onq

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spinqualitylabelsall models 1onq, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of CD1a in Complex with a Sulfatide

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

1ONQ is a Protein complex structure of sequences from Homo sapiens with FUC, NAG and SLF as ligands. Full crystallographic information is available from 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:12833155

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