Ontology highlight
ABSTRACT:
SUBMITTER: Reyes JP
PROVIDER: S-EPMC4594575 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Reyes J P JP Huanosta-Gutiérrez A A López-Rodríguez A A Martínez-Torres A A
Channels (Austin, Tex.) 20150101 2
We studied the effects of mutations of positively charged amino acid residues in the pore of X. tropicalis TMEM16A calcium-activated chloride channels: K613E, K628E, K630E; R646E and R761E. The activation and deactivation kinetics were not affected, and only K613E showed a lower current density. K628E and R761E affect anion selectivity without affecting Na(+) permeation, whereas K613E, R646E and the double mutant K613E + R646E affect anion selectivity and permeability to Na(+). Furthermore, alte ...[more]