1ihj
From Proteopedia
|
Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide
Overview
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, determined by both in vitro and in vivo studies. Since other proteins also, possess similar, cysteine-containing consensus sequences for binding PDZ, domains, this disulfide-mediated 'dock-and-lock' interaction of PDZ, domains with their ligands may be a relatively ubiquitous mode of, coordinating signaling pathways.
About this Structure
1IHJ is a Protein complex structure of sequences from Drosophila melanogaster. Active as Phospholipase C, with EC number 3.1.4.3 Full crystallographic information is available from OCA.
Reference
Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA., Kimple ME, Siderovski DP, Sondek J, EMBO J. 2001 Aug 15;20(16):4414-22. PMID:11500369
Page seeded by OCA on Tue Nov 20 17:24:05 2007
