Ontology highlight
ABSTRACT:
SUBMITTER: Hirano Y
PROVIDER: S-EPMC2856166 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Hirano Yoshinori Y Okimoto Noriaki N Kadohira Ikuko I Suematsu Makoto M Yasuoka Kenji K Yasui Masato M
Biophysical journal 20100401 8
Aquaporin (AQP) functions as a water-conducting pore. Mercury inhibits the water permeation through AQP. Although site-directed mutagenesis has shown that mercury binds to Cys189 during the inhibition process, it is not fully understood how this inhibits the water permeation through AQP1. We carried out 40 ns molecular dynamics simulations of bovine AQP1 tetramer with mercury (Hg-AQP1) or without mercury (Free AQP1). In Hg-AQP1, Cys191 (Cys189 in human AQP1) is converted to Cys-SHg+ in each mono ...[more]