Abstract
PDZ domains are protein modules manly found in metazoa. PDZ are about 90 residues long and were first found in proteins involved in signaling pathways. They have an important role in mediating interactions for the assembly of large multi protein complexes at specific subcellular locations. The ligand binds the domain in an extended conformation that serves as an additional beta strand. The main feature of PDZ-ligand interaction is that the C-terminal region of targets is specifically recognized.
Selected references
| Hata Y, Butz S, Sudhof TC | | CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
protein kinase domain identified by interaction with neurexins. | | J Neurosci 1996 Apr 15;16(8) : 2488-94. | | PMID: 8786425 |
| Hung AY, Sheng M | | PDZ domains: structural modules for protein complex assembly. | | J Biol Chem 2002 Feb 22;277(8) : 5699-702. | | PMID: 11741967 |
| Sheng M, Sala C | | PDZ domains and the organization of supramolecular complexes. | | Annu Rev Neurosci 2001;24() : 1-29. | | PMID: 11283303 |
| Torres R, Firestein BL, Dong H, Staudinger J, Olson EN, Huganir RL, Bredt DS, Gale NW, Yancopoulos GD | | PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors
and their ephrin ligands. | | Neuron 1998 Dec;21(6) : 1453-63. | | PMID: 9883737 |
This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.
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Biological Process |
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signal transduction
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Cellular Component |
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membrane |
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plasma membrane |
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cytosol |
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Molecular Function |
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protein binding |
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protein domain specific binding |
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pdz-domain binding |
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