PDZ domain

Molecular structure of the PDZ domain included in the human GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) protein
Identifiers
SymbolPDZ
PfamPF00595
InterProIPR001478
SMARTPDZ
PROSITEPDOC50106
SCOP21lcy / SCOPe / SUPFAM
CDDcd00136
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1l1jB:248-262 1lcyA:388-442 1fc7A:151-232

1fc9A:151-232 1fcfA:151-232 1fc6A:151-232 1ueqA:426-492 1ujvA:639-680 1i92A:14-91 1g9oA:14-91 1q3oA:663-754 1q3pA:663-754 1uepA:778-859 1wfvA:1147-1226 1uewA:920-1007 2cs5A:517-602 1qavA:81-161 2pdzA:81-161 1z86A:81-161 1z87A:81-161 1pdr :466-544 1tq3A:313-391 1be9A:313-391 1bfeA:313-391 1tp5A:313-391 1tp3A:313-391 1um7A:386-464 1iu2A:65-149 1iu0A:65-149 1kefA:65-149 1zokA:224-308 1qlcA:160-244 2bygA:193-277 2fe5A:226-310 1wi2A:47-125 1whaA:871-947 1x5qA: 728-812 1t2mA:993-1073 1um1A:974-1056 1wf8A:504-589 1gm1A:1357-1439 1oziA:1357-1439 1vj6A:1357-1439 1d5gA:1368-1450 3pdzA:1368-1450 1q7xA:1368-1450 1ujuA:1100-1189 1wi4A:22-94 1l6oA:254-339 1mc7A:251-336 1n7tA:1323-1407 1mfgA:1323-1407 1mflA:1323-1407 1uezA:140-219 1uf1A:279-357 1x5nA:211-289 1ihjA:17-103 1uhpA:249-336 1uitA:1240-1316 1x6dA:412-495 2csjA:10-94 1m5zA:988-1067 2cssA:605-688 1zubA:619-702 1wfgA:668-753 1ufxA:816-887 1qauA:17-96 1b8qA:17-96 1u38A:656-740 1u37A:656-740 1u3bA:656-740 1x45A:656-740 1p1dA:471-557 1p1eA:471-557 1x5rA:456-542 1v62A:248-329 1n7fA:672-751 1n7eA:672-751 1wf7A:5-82 1rgwA:4-81 1vb7A:3-81 1i16 :533-616 1v6bA:752-838 2f5yB:300-373 1whdA:18-92 1yboA:114-191 1v1tB:114-191 1obzB:114-191 1n99A:114-191 1wh1A:419-501 1va8A:256-333 1kwaA:490-568 1nf3D:157-247 1rzxA:160-250 1obyB:198-270 1obxA:198-270 1nteA:198-270 1r6jA:198-270 1u39A:747-820

1y7nA:747-820

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.

  1. ^ 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.
  2. ^ 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.
  3. ^ Cite error: The named reference pmid20509869 was invoked but never defined (see the help page).
  4. ^ 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.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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.
  8. ^ 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.