1IHJ

Crystal Structure of the N-terminal PDZ domain of InaD in complex with a NorpA C-terminal peptide

Summary for 1IHJ

• Entry DOI: 10.2210/pdb1ihj/pdb
• Descriptor: InaD, phospholipase C (3 entities in total)
• Functional Keywords: intermolecular disulfide bond, pdz domain, signaling protein
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Cell membrane; Peripheral membrane protein: Q24008
• Total number of polymer chains: 4
• Total formula weight: 23054.78

Authors

Kimple, M.E.,Siderovski, D.P.,Sondek, J. (deposition date: 2001-04-19, release date: 2001-08-22, Last modification date: 2023-08-16)

Primary citation

Kimple, M.E.,Siderovski, D.P.,Sondek, J.
Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA.
EMBO J., 20:4414-4422, 2001

PubMed 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 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.

PubMed: 11500369
DOI: 10.1093/emboj/20.16.4414

Experimental method

X-RAY DIFFRACTION (1.8 Å)