2bve | pdb_00002bve

STRUCTURE OF THE N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH 2-PHENYL-PROP5AC

spinqualitylabelsall models 2bve, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bve is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PH5 Related: 1od7, 1od9, 1oda, 1qfo, 1qfp, 1url Resources: FirstGlance, OCA, RCSB, PDBsum Function [SN_MOUSE] Acts as an endocytic receptor mediating clathrin dependent endocytosis. Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds to SPN/CD43 on T-cells. May play a role in hematopoiesis. May act as a counter-receptor for CLEC10A in lymph node. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-Neu5NAc. These structures reveal that SnD1 undergoes very few structural changes on ligand binding and detail how two novel classes of sialic acid analogs bind, one of which unexpectedly can induce Siglec dimerization. In conjunction with in silico analysis, this set of structures informs us about the design of putative ligands with enhanced binding affinities and specificities to different Siglecs, and provides data with which to test the effectiveness of different computational drug design protocols. Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin.,Zaccai NR, May AP, Robinson RC, Burtnick LD, Crocker PR, Brossmer R, Kelm S, Jones EY J Mol Biol. 2007 Feb 2;365(5):1469-79. Epub 2006 Oct 28. PMID:17137591 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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