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Structural views of phosphoinositide-specific phospholipase C: signalling the way ahead
1Centre for Protein Engineering, MRC Centre, Cambridge, UK. riw@mrc-lmb.cam.ac.uk
Structure (London, England : 1993)
|December 15, 1996
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.