Ontology highlight
ABSTRACT:
SUBMITTER: Khelashvili G
PROVIDER: S-EPMC6823365 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Khelashvili George G Falzone Maria E ME Cheng Xiaolu X Lee Byoung-Cheol BC Accardi Alessio A Weinstein Harel H
Nature communications 20191031 1
Both lipid and ion translocation by Ca<sup>2+</sup>-regulated TMEM16 transmembrane proteins utilizes a membrane-exposed hydrophilic groove. Several conformations of the groove are observed in TMEM16 protein structures, but how these conformations form, and what functions they support, remains unknown. From analyses of atomistic molecular dynamics simulations of Ca<sup>2+</sup>-bound nhTMEM16 we find that the mechanism of a conformational transition of the groove from membrane-exposed to occluded ...[more]