Epitopes described in "The crystal structure of human CD1b with a bound bacterial glycolipid."

Reference
Article Authors:Thil Batuwangala; Dawn Shepherd; Stephan D Gadola; Kevin J C Gibson; Nathan R Zaccai; Alan R Fersht; Gurdyal S Besra; Vincenzo Cerundolo; E Yvonne Jones
Article Title:The crystal structure of human CD1b with a bound bacterial glycolipid.
Reference Detail
Reference ID:1012874
Abstract:The human MHC class I-like molecule CD1b is distinctive among CD1 alleles in that it is capable of presenting a set of glycolipid species that show a very broad range of variation in the lengths of their acyl chains. A structure of CD1b complexed with relatively short acyl chain glycolipids plus detergent suggested how an interlinked network of channels within the Ag-binding groove could accommodate acyl chain lengths of up to 80 carbons. The structure of CD1b complexed with glucose monomycolate, reported in this study, confirms this hypothesis and illustrates how the distinctive substituents of intracellular bacterial glycolipids can be accommodated. The Ag-binding groove of CD1b is, uniquely among CD1 alleles, partitioned into channels suitable for the compact accommodation of lengthy acyl chains. The current crystal structure illustrates for the first time the binding of a natural bacterial lipid Ag to CD1b and shows how its novel structural features fit this molecule for its role in the immune response to intracellular bacteria.
Affiliations:Cancer Research UK Receptor Structure Group, The Division of Structural Biology, and Cancer Research UK.
Date:2004
Reference Type:Literature
PubMed ID:14764708
Journal:J Immunol
Journal Volume:172
Article Pages:2382-8
Journal ISSN:0022-1767
Article Chemical List:Antigens, Bacterial;Antigens, CD1;CD1b antigen;Glycolipids;Phosphatidylinositols;Protein Isoforms;Receptors, Antigen, T-Cell;glucose mycolate;G(M2) Ganglioside
Article MeSH List:Amino Acid Sequence; Antigen Presentation; Antigens, Bacterial(chemistry; immunology; metabolism); Antigens, CD1(chemistry; metabolism); Crystallography, X-Ray; G(M2) Ganglioside(chemistry); Glycolipids(chemistry; immunology; metabolism); Humans; Hydrophobic and Hydrophilic Interactions; Mass Spectrometry; Molecular Sequence Data; Nocardia(immunology); Phosphatidylinositols(chemistry); Protein Binding(immunology); Protein Folding; Protein Isoforms(chemistry); Receptors, Antigen, T-Cell(metabolism); Sequence Homology, Amino Acid
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