PDZ domain

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Molecular structure of the PDZ domain included in the human GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) protein.
Molecular structure of the PDZ domain included in the human GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) protein.

The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, and animals[1]. PDZ is an acronym combining the first letters of three proteins — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (DlgA), and zonula occludens-1 protein (zo-1) — which were first discovered to share the domain. PDZ domains are also referred to as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains. These domains help anchor transmembrane proteins to the cytoskeleton and hold together signaling complexes[2]. The folding and binding reactions of PDZ domains to their target ligands suggest that ligand binding

There are roughly 260 human PDZ domains, though since several PDZ domain containing proteins hold several domains, the actual number of PDZ proteins is closer to 180. Listed below are some of the better studied members of this family.


  1. ^ Ponting C (1997). "Evidence for PDZ domains in bacteria, yeast, and plants.". Protein Sci 6 (2): 464-8. PMID 9041651. 
  2. ^ Ranganathan R, Ross E (1997). "PDZ domain proteins: scaffolds for signaling complexes.". Curr Biol 7 (12): R770-3. PMID 9382826. 
  3. ^ Jemth, P., Gianni, S. (2007). "PDZ domains: folding and binding". Biochemistry 40 (30): 8701-8708. PMID 17620015. 

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