Interactions and cooperativity between P-glycoprotein structural domains determined by thermal unfolding provides insights into its solution structure and function
刊名:Biochimica et Biophysica Acta (BBA) - Biomembranes
出版年:2017
出版时间:January 2017
年:2017
卷:1859
期:1
页码:48-60
全文大小:1411 K
卷排序:1859
文摘
P-glycoprotein thermal unfolding data indicate two cooperative unfolding units. Each cooperative unit contains one NBD and two contacting intracellular loops. P-glycoprotein is predominantly inward-facing under continuous ATP hydrolysis. Outward-facing conformation in wild-type P-glycoprotein is transient. Outward-facing conformation is detected by DSC only when ATP hydrolysis is disabled.