Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA.

ABSTRACT: In Drosophila, phototransduction is mediated by G(q)-activation of phospholipase C and is a well studied model system for understanding the kinetics of signal initiation, propagation and termination controlled by G proteins. The proper intracellular targeting and spatial arrangement of most proteins involved in fly phototransduction require the multi-domain scaffolding protein InaD, composed almost entirely of five PDZ domains, which independently bind various proteins including NorpA, the relevant phospho lipase C-beta isozyme. We have determined the crystal structure of the N-terminal PDZ domain of InaD bound to a peptide corresponding to the C-terminus of NorpA to 1.8 A resolution. The structure highlights an intermolecular disulfide bond necessary for high affinity interaction as deter

SUBMITTER: Kimple ME 

PROVIDER: S-EPMC125561 | biostudies-literature | 2001 Aug

REPOSITORIES: biostudies-literature