6oor

Structure of 1B1 bound to mouse CD1d

spinqualitylabelsall models 6oor, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6oor is a 4 chain structure with sequence from Mus musculus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: NA, UNL 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. Publication Abstract from PubMed Natural killer T (NKT) cells are a subset of T lymphocytes that recognize glycolipid antigens presented by CD1d molecule (CD1d). They rapidly respond to antigen challenge and can activate both innate and adaptive immune cells. To study the role of antigen presentation in NKT cell activation, previous studies have developed several anti-CD1d antibodies that block CD1d binding to T-cell receptors (TCRs). Antibodies that are specific to both CD1d and the presented antigen can only be used to study the function of only a limited number of antigens. In contrast, antibodies that bind CD1d and block TCR binding regardless of the presented antigen can be widely used to assess the role of TCR-mediated NKT cell activation in various disease models. Here, we report the crystal structure of the widely used anti-mouse CD1d antibody 1B1 bound to CD1d at a resolution of 2.45A and characterized its binding to CD1d-presented glycolipids. We observed that 1B1 uses a long hydrophobic H3 loop that is inserted deep into the binding groove of CD1d where it makes intimate non-polar contacts with the lipid backbone of an incorporated spacer lipid. Using an NKT cell agonist that has a modified sphingosine moiety, we further demonstrate that 1B1 in its monovalent form cannot block TCR mediated NKT cell activation, since 1B1 fails to bind with high affinity to mCD1d. Our results suggest potential limitations of using 1B1 to assess antigen recognition by NKT cells, especially when investigating antigens that do not follow the canonical two-alkyl-chain rule. Structural basis of NKT cell inhibition using the T-cell receptor-blocking anti-CD1d antibody 1B1.,Ying G, Wang J, Mallevaey T, Van Calenbergh S, Zajonc DM J Biol Chem. 2019 Jul 11. pii: RA119.009403. doi: 10.1074/jbc.RA119.009403. PMID:31296659 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody 3D structures Beta-2 microglobulin 3D structures CD1 SARM1 3D structures 3D structures of non-human antibody

Proteopedia Page Contributors and Editors (what is this?)

OCA