5efi

Crystal structure of mouse CD1d in complex with the p99p lipopeptide

spinqualitylabelsall models 5efi, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5efi is a 3 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, CIT, FUC, MAN, NA, NAG, OCA, PLM Related: 5fkp Gene: Cd1d1, Cd1.1 (LK3 transgenic mice), B2m (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CD1D1_MOUSE] Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMed Mouse CD1d is a non-classical MHC molecule able to present lipids and glycolipids to a specialized subset of T cells known as Natural Killer T (NKT) cells. The antigens presented by CD1d has been shown to cover a broad range of chemical structures and to follow precise rules determining the potency of the antigen in the context of T cell activation. Together with lipids, initial reports suggested that CD1d can also bind and present hydrophobic peptides with a motif of the nature [FW]-X-X-[ILM]-X-X-W. However, the exact location of peptide binding and the molecular basis for the required motif are currently unknown. Here we present the crystal structure of the first peptide identified to bind CD1d, p99, and show that it binds in the antigen-binding groove of CD1d in a manner compatible with its presentation to T cell receptors. Interestingly, the peptide adopts an alpha-helical conformation, which orients the motif residues toward its deep binding groove, therefore explaining the molecular requirements for peptide binding. Moreover, we demonstrate that a lipopeptide version of the same peptide is able to bind CD1d in a similar conformation, identifying another class of molecules binding this antigen-presenting molecule. Structure of an alpha-helical peptide and lipopeptide bound to the non-classical MHC class I molecule CD1d.,Girardi E, Wang J, Zajonc DM J Biol Chem. 2016 Mar 22. pii: jbc.M115.702118. PMID:27006394 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures

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