1zt4

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Revision as of 18:34, 12 November 2007

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spinqualitylabelsall models 1zt4, resolution 3.000Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The crystal structure of human CD1d with and without alpha-Galactosylceramide

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The glycolipid alpha-galactosylceramide binds with high affinity to CD1d, and stimulates natural killer T cells. Here we report the crystal, structure of human CD1d in complex with synthetic alpha-galactosylceramide, at a resolution of 3.0 A. The structure shows a tightly fit lipid in the, CD1d binding groove, with the sphingosine chain bound in the C' pocket and, the longer acyl chain anchored in the A' pocket. We also present the CD1d, structure without lipid, which has a more open conformation of the binding, groove, suggesting a dual conformation of CD1d in which the 'open', conformation is more able to load lipids. These structures provide clues, as to how CD1 molecules load glycolipids as well as data to guide the, design of new therapeutic agents.

Disease

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

About this Structure

1ZT4 is a Protein complex structure of sequences from Homo sapiens with AGH as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of human CD1d with and without alpha-galactosylceramide., Koch M, Stronge VS, Shepherd D, Gadola SD, Mathew B, Ritter G, Fersht AR, Besra GS, Schmidt RR, Jones EY, Cerundolo V, Nat Immunol. 2005 Aug;6(8):819-26. Epub 2005 Jul 10. PMID:16007090

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