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3DX1

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

Summary for 3DX1
Entry DOI10.2210/pdb3dx1/pdb
Related1HTY 1HWW 1HXK 1PS2 1QWN 1R33 1R34 1TQV 2ALW 2F7O 2F7P 2F7Q 2F7R 2FYV 3BUB 3BUP 3CZN 3DX0 3DX2 3DX3 3DX4
DescriptorAlpha-mannosidase 2, 2-acetamido-2-deoxy-beta-D-glucopyranose, PHOSPHATE ION, ... (7 entities in total)
Functional Keywordsgh38 glycosidase, glycosidase, golgi apparatus, hydrolase, membrane, metal-binding, signal-anchor, transmembrane
Biological sourceDrosophila melanogaster (Fruit fly)
Total number of polymer chains1
Total formula weight120334.52
Authors
Kuntz, D.A.,Rose, D.R. (deposition date: 2008-07-23, release date: 2009-07-07, Last modification date: 2024-11-06)
Primary citationKuntz, D.A.,Zhong, W.,Guo, J.,Rose, D.R.,Boons, G.J.
The molecular basis of inhibition of Golgi alpha-mannosidase II by mannostatin A.
Chembiochem, 10:268-277, 2009
Cited by
PubMed Abstract: 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.
PubMed: 19101978
DOI: 10.1002/cbic.200800538
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.21 Å)
Structure validation

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