作者: Angeline M. Lyon , Jessica A. Begley , Taylor D. Manett , John J.G. Tesmer
DOI: 10.1016/J.STR.2014.10.008
关键词:
摘要: Phospholipase C β (PLCβ) enzymes are dramatically activated by heterotrimeric G proteins. Central to this response is the robust autoinhibition of PLCβ X-Y linker region within its catalytic core and Hα2' helix in C-terminal extension enzyme. The molecular mechanism each their mutual dependence poorly understood. Herein, it shown that distinct regions have specific roles regulating activity. Most important,an acidic stretch stabilizes a lid occludes active site, consistent with crystal structures variants lacking region. Inhibition independent likely regulates activity limiting membrane interaction core. Full activation thus requires multiple events induced association binding regulatory