Williams R L, Katan M
Centre for Protein Engineering, MRC Centre, Cambridge, UK.
Structure. 1996 Dec 15;4(12):1387-94. doi: 10.1016/s0969-2126(96)00146-3.
Recent structural studies of mammalian phosphoinositide-specific phospholipase C (PI-PLC) have begun to shed light on the mechanism whereby this family of effector enzymes is able to hydrolyze phospholipid substrates to yield second messengers. PI-PLC isozymes employ a variety of modules (PH domain, EF-hand domain, SH2 domain, SH3 domain and C2 domain) that are common in proteins involved in signal transduction to reversibly interact with membranes and protein components of the signalling pathways.
近期对哺乳动物磷酸肌醇特异性磷脂酶C（PI-PLC）的结构研究已开始揭示这类效应酶能够水解磷脂底物以产生第二信使的机制。PI-PLC同工酶利用多种模块（PH结构域、EF手结构域、SH2结构域、SH3结构域和C2结构域），这些模块在参与信号转导的蛋白质中很常见，用于与信号通路的膜和蛋白质成分进行可逆相互作用。
