1HTY

GOLGI ALPHA-MANNOSIDASE II

1HTY の概要

• エントリーDOI: 10.2210/pdb1hty/pdb
• 分子名称: ALPHA-MANNOSIDASE II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (6 entities in total)
• 機能のキーワード: n-terminal alpha-beta domain, three helix bundle, 2 c-terminal beta barrels, hydrolase
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 117969.02

構造登録者

van den Elsen, J.M.H.,Kuntz, D.A.,Rose, D.R. (登録日: 2001-01-02, 公開日: 2002-01-02, 最終更新日: 2024-10-30)

主引用文献

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

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: 11406577
DOI: 10.1093/emboj/20.12.3008

実験手法

X-RAY DIFFRACTION (1.4 Å)