3dx1 | pdb_00003dx1

Golgi alpha-Mannosidase II in complex with Mannostatin analog (1S,2S,3R,4R)-4-aminocyclopentane-1,2,3-triol

spinqualitylabelsall models 3dx1, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dx1 is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MRD, NAG, PO4, YHO, ZN Related: 1hty, 1hww, 1hxk, 1ps2, 1qwn, 1r33, 1r34, 1tqv, 2alw, 2f7o, 2f7p, 2f7q, 2f7r, 2fyv, 3bub, 3bup, 3czn, 3dx0, 3dx2, 3dx3, 3dx4 Gene: alpha-Man-II, GmII, CG18802 (Drosophila melanogaster) Activity: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, with EC number 3.2.1.114 Resources: FirstGlance, OCA, RCSB, PDBsum Function [MAN2_DROME] Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity). 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 Mannostatin A is a potent inhibitor of the mannose-trimming enzyme, Golgi alpha-mannosidase II (GMII), which acts late in the N-glycan processing pathway. Inhibition of this enzyme provides a route to blocking the transformation-associated changes in cancer cell surface oligosaccharide structures. Here, we report on the synthesis of new Mannostatin derivatives and analyze their binding in the active site of Drosophila GMII by X-ray crystallography. The results indicate that the interaction with the backbone carbonyl of Arg876 is crucial to the high potency of the inhibitor-an effect enhanced by the hydrophobic interaction between the thiomethyl group and an aromatic pocket vicinal to the cleavage site. The various structures indicate that differences in the hydration of protein-ligand complexes are also important determinants of plasticity as well as selectivity of inhibitor binding. The molecular basis of inhibition of Golgi alpha-mannosidase II by mannostatin A.,Kuntz DA, Zhong W, Guo J, Rose DR, Boons GJ Chembiochem. 2009 Jan 26;10(2):268-77. PMID:19101978 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mannosidase

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