 Molecular structure of the PDZ domain included in the human GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) protein | |||||||||||
| Identifiers | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Symbol | PDZ | ||||||||||
| Pfam | PF00595 | ||||||||||
| InterPro | IPR001478 | ||||||||||
| SMART | PDZ | ||||||||||
| PROSITE | PDOC50106 | ||||||||||
| SCOP2 | 1lcy / SCOPe / SUPFAM | ||||||||||
| CDD | cd00136 | ||||||||||
| |||||||||||
The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses[1] and animals.[2] Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. Proteins with these domains help hold together and organize signaling complexes at cellular membranes. These domains play a key role in the formation and function of signal transduction complexes.[3] PDZ domains also play a highly significant role in the anchoring of cell surface receptors (such as Cftr and FZD7) to the actin cytoskeleton via mediators like NHERF and ezrin.[4]
PDZ is an initialism combining the first letters of the first three proteins discovered to share the domain — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1).[5] PDZ domains have previously been referred to as DHR (Dlg homologous region)[6] or GLGF (glycine-leucine-glycine-phenylalanine) domains.[7]
In general PDZ domains bind to a short region of the C-terminus of other specific proteins. These short regions bind to the PDZ domain by beta sheet augmentation. This means that the beta sheet in the PDZ domain is extended by the addition of a further beta strand from the tail of the binding partner protein.[8] The C-terminal carboxylate group is bound by a nest (protein structural motif) in the PDZ domain, i.e. a PDZ-binding motif.
- ^ Boxus M, Twizere JC, Legros S, Dewulf JF, Kettmann R, Willems L (August 2008). "The HTLV-1 Tax interactome". Retrovirology. 5: 76. doi:10.1186/1742-4690-5-76. PMC 2533353. PMID 18702816.
- ^ Ponting CP (February 1997). "Evidence for PDZ domains in bacteria, yeast, and plants". Protein Science. 6 (2): 464–8. doi:10.1002/pro.5560060225. PMC 2143646. PMID 9041651.
- ^ Cite error: The named reference
pmid20509869was invoked but never defined (see the help page). - ^ Li J, Callaway DJ, Bu Z (September 2009). "Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1". Journal of Molecular Biology. 392 (1): 166–80. doi:10.1016/j.jmb.2009.07.005. PMC 2756645. PMID 19591839.
- ^ Kennedy MB (September 1995). "Origin of PDZ (DHR, GLGF) domains". Trends in Biochemical Sciences. 20 (9): 350. doi:10.1016/S0968-0004(00)89074-X. PMID 7482701.
- ^ Ponting CP, Phillips C (March 1995). "DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins". Trends in Biochemical Sciences. 20 (3): 102–3. doi:10.1016/S0968-0004(00)88973-2. PMID 7535955.
- ^ Cho KO, Hunt CA, Kennedy MB (November 1992). "The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein". Neuron. 9 (5): 929–42. doi:10.1016/0896-6273(92)90245-9. PMID 1419001. S2CID 28528759.
- ^ Cowburn D (December 1997). "Peptide recognition by PTB and PDZ domains". Current Opinion in Structural Biology. 7 (6): 835–8. doi:10.1016/S0959-440X(97)80155-8. PMID 9434904.