Targeting the Protein Tunnels of the Urease Accessory Complex: A Theoretical Investigation.

ABSTRACT: Urease is a nickel-containing enzyme that is essential for the survival of several and often deadly pathogenic bacterial strains, including Helicobacter pylori. Notwithstanding several attempts, the development of direct urease inhibitors without side effects for the human host remains, to date, elusive. The recently solved X-ray structure of the HpUreDFG accessory complex involved in the activation of urease opens new perspectives for structure-based drug discovery. In particular, the quaternary assembly and the presence of internal tunnels for nickel translocation offer an intriguing possibility to target the HpUreDFG complex in the search of indirect urease inhibitors. In this work, we adopted a theoretical framework to investigate such a hypothesis. Specifically, w

SUBMITTER: Masetti M 

PROVIDER: S-EPMC7355429 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature