title: Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead.
abstract: 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.
authors.affiliation: Centre for Protein Engineering, MRC Centre, Cambridge, UK. riw@mrc-lmb.cam.ac.uk
authors.forename: R L
authors.initials: RL
authors.lastname: Williams
authors.forename: M
authors.initials: M
authors.lastname: Katan
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology; D010738:Type C Phospholipases / Q000737:chemistry* / Q000145:classification
chemical_list: D007527:Isoenzymes; D010716:Phosphatidylinositols; D010738:Type C Phospholipases; D002118:Calcium