Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1862, Issue 6, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2020.183202
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Funding
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN-2015-05372]
- Heart and Stroke Foundation of Canada [G-18-0022076]
- Canadian Graduate Scholarship-Master's Program scholarship from NSERC
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ATP binding cassette (ABC) proteins are a large family of membrane proteins present in all kingdoms of life. These multi-domain proteins are comprised, at minimum, of two membrane-spanning domains (MSD1, MSD2) and two cytosolic nucleotide binding domains (NBD1, NBD2). ATP binding and hydrolysis at the NBDs enables ABC proteins to actively transport solutes across membranes, regulate activities of other proteins, or function as channels. Like most eukaryotic membrane proteins, ABC proteins contain intrinsically disordered regions (IDRs). These conformationally dynamic regions in ABC proteins possess residual structure, are sites of phosphorylation, and mediate protein-protein interactions. Here, we review the role of IDRs in regulating ABC protein activity.
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