The crystal structure of human CD1d with and without alpha-galactosylceramide.

Abstract:

: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.

journal_name

Nat Immunol

journal_title

Nature immunology

authors

Koch M,Stronge VS,Shepherd D,Gadola SD,Mathew B,Ritter G,Fersht AR,Besra GS,Schmidt RR,Jones EY,Cerundolo V

doi

10.1038/ni1225

keywords:

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

819-26

issue

8

eissn

1529-2908

issn

1529-2916

pii

ni1225

journal_volume

6

pub_type

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