Binding of Vac14 to neuronal nitric oxide synthase: Characterisation of a new internal PDZ-recognition motif

24Citations
Citations of this article
17Readers
Mendeley users who have this article in their library.

Abstract

PDZ domains mediate protein interactions primarily through either classical recognition of carboxyl-terminal motifs or PDZ/PDZ domain associations. Several studies have also described internal modes of PDZ recognition, most of which depend on β-finger structures. Here, we describe a novel interaction between the PDZ domain of nNOS and Vac14, the activator of the PtdIns(3)P 5-kinase PIKfyve. Binding assays using various Vac14 deletion constructs revealed a β-finger independent interaction that is based on a novel internal motif. Mutational analyses reveal essential residues within the motif allowing us to define a new type of PDZ domain interaction. © 2006 Federation of European Biochemical Societies.

Cite

CITATION STYLE

APA

Lemaire, J. F., & McPherson, P. S. (2006). Binding of Vac14 to neuronal nitric oxide synthase: Characterisation of a new internal PDZ-recognition motif. FEBS Letters, 580(30), 6948–6954. https://doi.org/10.1016/j.febslet.2006.11.061

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free