Self-recognition by an intrinsically disordered protein

Hecht, Oliver, Ridley, Helen, Boetzel, Ruth, Lewin, Allison, Cull, Nick, Chalton, David A., Lakey, Jeremy H. and Moore, Geoffrey R. (2008) Self-recognition by an intrinsically disordered protein. FEBS Letters, 582 (17). pp. 2673-7. ISSN 0014-5793

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The intrinsically disordered translocation domain (T-domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T-domain of colicin N known to bind to the helper protein TolA in target cells also interacts intramolecularly with folded regions of colicin N. We suggest that this specific self-recognition helps intrinsically disordered domains to bury their hydrophobic recognition motifs and protect them against degradation, showing that an impaired self-recognition leads to increased protease susceptibility.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009)
Depositing User: Users 2731 not found.
Date Deposited: 14 Mar 2012 15:11
Last Modified: 24 Oct 2022 00:40
DOI: 10.1016/j.febslet.2008.06.022

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