ArticleJournal of immunology (Baltimore, Md. : 1950)2010
Crystal structure of bovine CD1b3 with endogenously bound ligands.
Article in Journal of immunology (Baltimore, Md. : 1950), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Mammalian CD1 and MR1 genes.Immunogenetics · 2016Review
- The CD1 family: serving lipid antigens to T cells since the Mesozoic era.Immunogenetics · 2016Review
- Coevolution of T-cell receptors with MHC and non-MHC ligands.Immunological reviews · 2015Review
- CD1 and mycobacterial lipids activate human T cells.Immunological reviews · 2015Review
- Recognition of Microbial Glycolipids by Natural Killer T Cells.Frontiers in immunology · 2015Review
- Expression patterns of bovine CD1 in vivo and assessment of the specificities of the anti-bovine CD1 antibodies.PloS one · 2015Article
- Automated identification of crystallographic ligands using sparse-density representations.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Dynamics of the antigen-binding grooves in CD1 proteins: reversible hydrophobic collapse in the lipid-free state.The Journal of biological chemistry · 2013Article
- Crystal structures of bovine CD1d reveal altered αGalCer presentation and a restricted A' pocket unable to bind long-chain glycolipids.PloS one · 2012Article
- Structural reorganization of the antigen-binding groove of human CD1b for presentation of mycobacterial sulfoglycolipids.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Crystal structure of human CD1e reveals a groove suited for lipid-exchange processes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Structure of a classical MHC class I molecule that binds "non-classical" ligands.PLoS biology · 2010Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
The CD1 family of Ag-presenting molecules is able to display lipids to T cells by binding them within a hydrophobic groove connected to the protein surface. In particular, the CD1b isotype is capable of binding ligands with greatly varying alkyl chain lengths through a complex network of interconnected hydrophobic pockets. Interestingly, mycobacterial lipids such as glucose monomycolate exclusively bind to CD1b. We determined the crystal structure of one of the three expressed bovine CD1b proteins, CD1b3, in complex with endogenous ligands, identified by mass spectrometry as a mixture of phosphatidylcholine and phosphatidylethanolamine, and analyzed the ability of the protein to bind glycolipids in vitro. The structure reveals a complex binding groove architecture, similar to the human ortholog but with consequential differences. Intriguingly, in bovine CD1b3 only the A', C' and F' pockets are present, whereas the T' pocket previously described in human CD1b is closed. This different pocket conformation could affect the ability of boCD1b3 to recognize lipids with long acyl chains such as glucose monomycolate. However, even in the absence of a T' tunnel, bovine CD1b3 is able to bind mycolates from Rhodococcus ruber in vitro.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.