2wml | pdb_00002wml

CRYSTAL STRUCTURE OF A MAMMALIAN SIALYLTRANSFERASE

spinqualitylabelsall models 2wml, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wml is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. Ligands: CL, GOL NonStd Res: MSE Related: 2wnb, 2wnf Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum 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 Mammalian cell surfaces are modified by complex arrays of glycoproteins, glycolipids and polysaccharides, many of which terminate in sialic acid and have central roles in essential processes including cell recognition, adhesion and immunogenicity. Sialylation of glycoconjugates is performed by a set of sequence-related enzymes known as sialyltransferases (STs). Here we present the crystal structure of a mammalian ST, porcine ST3Gal-I, providing a structural basis for understanding the mechanism and specificity of these enzymes and for the design of selective inhibitors. Structural insight into mammalian sialyltransferases.,Rao FV, Rich JR, Rakic B, Buddai S, Schwartz MF, Johnson K, Bowe C, Wakarchuk WW, Defrees S, Withers SG, Strynadka NC Nat Struct Mol Biol. 2009 Nov;16(11):1186-8. Epub 2009 Oct 11. PMID:19820709 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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