Conference Proceedings
Crystal structures and computer screened inhibitors of Helicobacter pylori undecaprenyl pyrophosphate synthase
Chih-Jung Kuo, Rey-Ting Guo, I-Lin Lu, Hong-Gi Liu, Su-Ying Wu, Tzu-Ping Ko, Andrew H-J Wang, Po-Huang Liang, D Howard (ed.), PK Rhee (ed.), S Halgamuge (ed.), SJ Yoo (ed.)
PROCEEDINGS OF THE FRONTIERS IN THE CONVERGENCE OF BIOSCIENCE AND INFORMATION TECHNOLOGIES | IEEE COMPUTER SOC | Published : 2007
DOI: 10.1109/FBIT.2007.34
Abstract
Helicobacter Pylori colonizes the human gastric epithelium and causes diseases such as gastritis, peptic ulcers, and stomach cancer. Undecaprenyl pyrophosphate synthase (UPPs), which catalyzes consecutive condensation reactions of farnesyl pyrophosphate with eight isopentenyl pyrophosphate to form lipid carrier for bacterial peptidoglycan biosynthesis, represents a potential target for developing new antibiotics. In the present study, X-ray structural analysis and computer virtual screening of inhibitors were performed for H. pylori UPPs. The 3-D structure of H. pylori UPPs was solved, with subtle variations from that of E. coli UPPs. Using the structures, two hits identified from 58,635 com..
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