Ontology highlight
ABSTRACT:
SUBMITTER: Kalienkova V
PROVIDER: S-EPMC6414200 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
Kalienkova Valeria V Clerico Mosina Vanessa V Bryner Laura L Oostergetel Gert T GT Dutzler Raimund R Paulino Cristina C
eLife 20190221
Scramblases catalyze the movement of lipids between both leaflets of a bilayer. Whereas the X-ray structure of the protein nhTMEM16 has previously revealed the architecture of a Ca<sup>2+</sup>-dependent lipid scramblase, its regulation mechanism has remained elusive. Here, we have used cryo-electron microscopy and functional assays to address this question. Ca<sup>2+</sup>-bound and Ca<sup>2+</sup>-free conformations of nhTMEM16 in detergent and lipid nanodiscs illustrate the interactions with ...[more]