A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles.
The Journal Of Biological Chemistry
Sarkar, Samantha K SK; Foo, Alexander C Y ACY; Matyas, Angela A; Asikhia, Ikhuosho I; Kosenko, Tanja T; Goto, Natalie K NK; Vergara-Jaque, Ariela A; Lagace, Thomas A TA
The M2 module of the Cys-His-rich domain (CHRD) of PCSK9 protein is needed for the extracellular low-density lipoprotein receptor (LDLR) degradation pathway.
The Journal Of Biological Chemistry
Saavedra, Yascara Grisel Luna YG; Day, Robert R; Seidah, Nabil G NG
Evidence for positive selection in the C-terminal domain of the cholesterol metabolism gene PCSK9 based on phylogenetic analysis in 14 primate species.