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Domain binding and function: PDZ domains bind to the C-terminal 4À5 residues of their target proteins, frequently transmembrane receptors or ion channels. These interactions can be of high affinity (nM Kd). The consensus binding sequence contains a hydrophobic residue, commonly Val or Ile, at the very C-terminus. Residues at the À2 and À3 positions are important in determining specificity. PDZ domains can also heterodimerize with PDZ domains of different proteins, potentially regulating intracellular signaling. In addition to engaging in protein-protein interactions, several PDZ domains including those of syntenin, CASK, Tiam1 and FAP are capable of binding to the phosphoinositide PIP2. PIP2-PDZ domain binding is thought to control the association of PDZ domain-containing proteins with the plasma membrane. Structure Reference: Doyle, D.A. et al. (1996) Cell 85(7), 1067À1076. Examples of Domain Proteins:

The third PDZ domain from PSD-95.

Binding Examples:

	PDZ domain proteins		Binding partners		domain binding sites
	Post-synaptic Density Protein 95 (PSD-95)		NMDA receptor B via PDZ1 and PDZ2 of PSD-95		– IESDV-COOH
	Post-synaptic Density Protein 95 (PSD-95)		Kvl1.4 Shaker-type K+ channel via PDZ1 and PDZ2 of PSD-95		– VETDV-COOH
	Post-synaptic Density Protein 95 (PSD-95)		Neural Nitric Oxide Synthase (nNOS) via PDZ2		PDZ/PDZ interaction