Abstract
▪ Abstract PDZ domains are modular protein interaction domains that bind in a sequence-specific fashion to short C-terminal peptides or internal peptides that fold in a β-finger. The diversity of PDZ binding specificities can be explained by variable amino acids lining the peptide-binding groove of the PDZ domain. Abundantly represented in Caenorhabditis elegans, Drosophila melanogaster, and mammalian genomes, PDZ domains are frequently found in multiple copies or are associated with other protein-binding motifs in multidomain scaffold proteins. PDZ-containing proteins are typically involved in the assembly of supramolecular complexes that perform localized signaling functions at particular subcellular locations. Organization around a PDZ-based scaffold allows the stable localization of interacting proteins and enhances the rate and fidelity of signal transduction within the complex. Some PDZ-containing proteins are more dynamically regulated in distribution and may also be involved in the trafficking of interacting proteins within the cell.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 27, 2002, 7:45 a.m.) |
Deposited | 3 years, 10 months ago (Oct. 14, 2021, 10:36 p.m.) |
Indexed | 2 days, 17 hours ago (Aug. 26, 2025, 3:15 a.m.) |
Issued | 24 years, 5 months ago (March 1, 2001) |
Published | 24 years, 5 months ago (March 1, 2001) |
Published Print | 24 years, 5 months ago (March 1, 2001) |
@article{Sheng_2001, title={PDZ Domains and the Organization of Supramolecular Complexes}, volume={24}, ISSN={1545-4126}, url={http://dx.doi.org/10.1146/annurev.neuro.24.1.1}, DOI={10.1146/annurev.neuro.24.1.1}, number={1}, journal={Annual Review of Neuroscience}, publisher={Annual Reviews}, author={Sheng, Morgan and Sala, Carlo}, year={2001}, month=mar, pages={1–29} }