Ontology highlight
ABSTRACT:
SUBMITTER: Kodan A
PROVIDER: S-EPMC3964115 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Kodan Atsushi A Yamaguchi Tomohiro T Nakatsu Toru T Sakiyama Keita K Hipolito Christopher J CJ Fujioka Akane A Hirokane Ryo R Ikeguchi Keiji K Watanabe Bunta B Hiratake Jun J Kimura Yasuhisa Y Suga Hiroaki H Ueda Kazumitsu K Kato Hiroaki H
Proceedings of the National Academy of Sciences of the United States of America 20140303 11
P-glycoprotein is an ATP-binding cassette multidrug transporter that actively transports chemically diverse substrates across the lipid bilayer. The precise molecular mechanism underlying transport is not fully understood. Here, we present crystal structures of a eukaryotic P-glycoprotein homolog, CmABCB1 from Cyanidioschyzon merolae, in two forms: unbound at 2.6-Å resolution and bound to a unique allosteric inhibitor at 2.4-Å resolution. The inhibitor clamps the transmembrane helices from the o ...[more]