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Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead Williams RL; Katan MStructure 1996[Dec]; 4 (12): 1387-94Recent 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.|Binding Sites[MESH]|Calcium/pharmacology[MESH]|Isoenzymes/chemistry/metabolism[MESH]|Models, Molecular[MESH]|Phosphatidylinositols/metabolism[MESH]|Protein Binding[MESH]|Protein Structure, Tertiary[MESH]|Signal Transduction/physiology[MESH]|Type C Phospholipases/*chemistry/classification[MESH] |
