6pws

Crystal structure of the cow C-type carbohydrate-recognition domain of CD23 in the presence of alpha-methyl mannoside

spinqualitylabelsall models 6pws, resolution 1.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pws is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1Å Ligands: CA, MMA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E1BIQ4_BOVIN Publication Abstract from PubMed CD23, the low-affinity IgE receptor found on B lymphocytes and other cells, contains a C-terminal lectin-like domain that resembles C-type carbohydrate-recognition domains (CRDs) found in many glycan-binding receptors. In most mammalian species, the CD23 residues required to form a sugar-binding site are present, although binding of CD23 to IgE does not involve sugars. Solid-phase binding competition assays, glycoprotein blotting experiments, and glycan array analysis employing the lectin-like domains of cow and mouse CD23 demonstrate that they bind to mannose, GlcNAc, glucose, and fucose and to glycoproteins that bear these sugars in nonreducing terminal positions. Crystal structures of the cow CRD in the presence of alpha-methyl mannoside and GlcNAcbeta1-2Man reveal that a range of oligosaccharide ligands can be accommodated in an open binding site in which most interactions are with a single terminal sugar residue. Although mouse CD23 shows a pattern of monosaccharide and glycoprotein binding similar to cow CD23, the binding is weaker. In contrast, no sugar binding was observed in similar experiments with human CD23. The absence of sugar-binding activity correlates with accumulation of mutations in the gene for CD23 in the primate lineage leading to humans, resulting in loss of key sugar-binding residues. These results are consistent with a role for CD23 in many species as a receptor for potentially pathogenic microorganisms as well as IgE. However, the ability of CD23 to bind several different ligands varies between species, suggesting that it has distinct functions in different organisms. CD23 is a glycan-binding receptor in some mammalian species.,Jegouzo SAF, Feinberg H, Morrison AG, Holder A, May A, Huang Z, Jiang L, Lasanajak Y, Smith DF, Werling D, Drickamer K, Weis WI, Taylor ME J Biol Chem. 2019 Oct 11;294(41):14845-14859. doi: 10.1074/jbc.RA119.010572. Epub, 2019 Sep 5. PMID:31488546 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CD23

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