Epitopes described in "The 2.5 Å structure of CD1c in complex with a mycobacterial lipid reveals an open groove ideally suited for diverse antigen presentation."

Reference
Article Authors:Louise Scharf; Nan-Sheng Li; Andrew J Hawk; Diana Garzón; Tejia Zhang; Lisa M Fox; Allison R Kazen; Sneha Shah; Esmael J Haddadian; Jenny E Gumperz; Alan Saghatelian; José D Faraldo-Gómez; Stephen C Meredith; Joseph A Piccirilli; Erin J Adams
Article Title:The 2.5 Å structure of CD1c in complex with a mycobacterial lipid reveals an open groove ideally suited for diverse antigen presentation.
Reference Detail
Reference ID:1021187
Abstract:CD1 molecules function to present lipid-based antigens to T cells. Here we present the crystal structure of CD1c at 2.5 Å resolution, in complex with the pathogenic Mycobacterium tuberculosis antigen mannosyl-1-phosphomycoketide (MPM). CD1c accommodated MPM's methylated alkyl chain exclusively in the A' pocket, aided by a unique exit portal underneath the 1 helix. Most striking was an open F' pocket architecture lacking the closed cavity structure of other CD1 molecules, reminiscent of peptide binding grooves of classical major histocompatibility complex molecules. This feature, combined with tryptophan-fluorescence quenching during loading of a dodecameric lipopeptide antigen, provides a compelling model by which both the lipid and peptide moieties of the lipopeptide are involved in CD1c presentation of lipopeptides.
Date:2010
Reference Type:Literature
PubMed ID:21167756
Journal:Immunity
Journal Volume:33
Article Pages:853-62
Journal ISSN:1074-7613
Article Chemical List:Antigens, Bacterial;Antigens, CD1;CD1C protein, human;Glycoproteins;Histocompatibility Antigens;Peptide Fragments
Article MeSH List:Antigen Presentation; Antigenic Variation; Antigens, Bacterial(chemistry; immunology); Antigens, CD1(chemistry; immunology); Cloning, Molecular; Computational Biology; Crystallization; Glycoproteins(chemistry; immunology); Histocompatibility Antigens(metabolism); Humans; Models, Immunological; Mycobacterium tuberculosis(immunology); Peptide Fragments(metabolism); Protein Binding; Protein Conformation; X-Rays
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