TAILIEUCHUNG - Báo cáo khoa học: Redox-regulated affinity of the third PDZ domain in the phosphotyrosine phosphatase PTP-BL for cysteine-containing target peptides

PDZ domains are protein–protein interaction modules that are crucial for the assembly of structural and signalling complexes. They specifically bind to short C-terminal peptides and occasionally to internal sequences that structurally resemble such peptide termini. The binding of PDZ domains is dominated by the residues at the P 0 and P )2 position within these C-ter-minal targets, but other residues are also important in determining specific-ity. | iFEBS Journal Redox-regulated affinity of the third PDZ domain in the phosphotyrosine phosphatase PTP-BL for cysteine-containing target peptides Lieke C. J. van den Berk1 Elena Landi2 Etelka Harmsen1 Luciana Dente2 and Wiljan J. A. J. Hendriks1 1 Department of Cell Biology Nijmegen Center for Molecular Life Sciences Radboud University Nijmegen the Netherlands 2 Dipartimento di Fisiologia e Biochimica Laboratorio di Biologia Cellulare e dello Sviluppo Universita di Pisa Italy Keywords disulfide bridge phage display proteinprotein interaction signal transduction surface plasmon resonance Correspondence . Hendriks Department of Cell Biology Nijmegen Center for Molecular Life Sciences Radboud University Nijmegen Geert Grooteplein 28 6525 GA Nijmegen the Netherlands Fax 31 24 361 5317 Tel 31 24 361 4329 E-mail Note . van den Berk and E. Landi contributed equally to this work Received 28 February 2005 revised 6 April 2005 accepted 28 April 2005 PDZ domains are protein-protein interaction modules that are crucial for the assembly of structural and signalling complexes. They specifically bind to short C-terminal peptides and occasionally to internal sequences that structurally resemble such peptide termini. The binding of PDZ domains is dominated by the residues at the P0 and P 2 position within these C-ter-minal targets but other residues are also important in determining specificity. In this study we analysed the binding specificity of the third PDZ domain of protein tyrosine phosphatase BAS-like PTP-BL using a C-ter-minal combinatorial peptide phage library. Binding of PDZ3 to C-termini is preferentially governed by two cysteine residues at the P 1 and P 4 position and a valine residue at the P0 position. Interestingly we found that this binding is lost upon addition of the reducing agent dithiothrietol indicating that the interaction is disulfide-bridge-dependent. Site-directed mutagenesis of the single cysteine residue in PDZ3 .

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