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1zt4
From Proteopedia
The crystal structure of human CD1d with and without alpha-Galactosylceramide
Contents |
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. 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 Page seeded by OCA on Sun Apr 13 08:16:48 2008
Categories: Homo sapiens | Protein complex | Besra, G S. | Cerundolo, V. | Fersht, A R. | Gadola, S D. | Jones, E Y. | Koch, M. | Mathew, B. | Ritter, G. | SPINE, Structural Proteomics in Europe. | Schmidt, R R. | Shepherd, D. | Stronge, V S. | Alpha-galactosylceramide | Alpha-galcer | Cd1 | Empty binding groove | Glycolipid | Human cd1d | Mhc class i | Spine | Structural genomic | Structural proteomics in europe
