1HTY
GOLGI ALPHA-MANNOSIDASE II
Summary for 1HTY
| Entry DOI | 10.2210/pdb1hty/pdb |
| Descriptor | ALPHA-MANNOSIDASE II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total) |
| Functional Keywords | n-terminal alpha-beta domain, three helix bundle, 2 c-terminal beta barrels, hydrolase |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 117969.02 |
| Authors | van den Elsen, J.M.H.,Kuntz, D.A.,Rose, D.R. (deposition date: 2001-01-02, release date: 2002-01-02, Last modification date: 2024-10-30) |
| Primary citation | van den Elsen, J.M.,Kuntz, D.A.,Rose, D.R. Structure of Golgi alpha-mannosidase II: a target for inhibition of growth and metastasis of cancer cells. EMBO J., 20:3008-3017, 2001 Cited by PubMed Abstract: Golgi alpha-mannosidase II, a key enzyme in N-glycan processing, is a target in the development of anti- cancer therapies. The crystal structure of Drosophila Golgi alpha-mannosidase II in the absence and presence of the anti-cancer agent swainsonine and the inhibitor deoxymannojirimycin reveals a novel protein fold with an active site zinc intricately involved both in the substrate specificity of the enzyme and directly in the catalytic mechanism. Identification of a putative GlcNAc binding pocket in the vicinity of the active site cavity provides a model for the binding of the GlcNAcMan(5)GlcNAc(2) substrate and the consecutive hydrolysis of the alpha1,6- and alpha1,3-linked mannose residues. The enzyme-inhibitor interactions observed provide insight into the catalytic mechanism, opening the door to the design of novel inhibitors of alpha-mannosidase II. PubMed: 11406577DOI: 10.1093/emboj/20.12.3008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
