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

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 beta-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 beta-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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Cell Line, Humans, Membrane Proteins, Molecular Sequence Data, Nitric Oxide Synthase Type I, Protein Binding
FEBS Lett.
Date: Dec. 22, 2006
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