ArticleStructure (London, England : 1993)2013
The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- The Power of Protein Dynamics in Binding and Allostery.Biochemistry · 2026Review
- Relative Binding Free Energy Estimation of Congeneric Ligands and Macromolecular Mutants with the Alchemical Transfer Method with Coordinate Swapping.Journal of chemical information and modeling · 2025Article
- GOPC facilitates the sorting of syndecan-1 in polarized epithelial cells.Molecular biology of the cell · 2022Article
- Free Energy-Based Computational Methods for the Study of Protein-Peptide Binding Equilibria.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structural basis of the human Scribble-Vangl2 association in health and disease.The Biochemical journal · 2021Article
- Phosphorylation-induced changes in the PDZ domain of Dishevelled 3.Scientific reports · 2021Article
- Computational Design of PDZ-Peptide Binding.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A Fluorescence-Based Assay to Determine PDZ-Ligand Binding Thermodynamics.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Syndecan-4/PAR-3 signaling regulates focal adhesion dynamics in mesenchymal cells.Cell communication and signaling : CCS · 2020Article
- Specificity in PDZ-peptide interaction networks: Computational analysis and review.Journal of structural biology: X · 2020Review
- SGEF forms a complex with Scribble and Dlg1 and regulates epithelial junctions and contractility.The Journal of cell biology · 2019Article
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- Conformational Dynamics and Cooperativity Drive the Specificity of a Protein-Ligand Interaction.Biophysical journal · 2019Article
- Article
- Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019Review
- Proteome-wide analysis of phospho-regulated PDZ domain interactions.Molecular systems biology · 2018Article
- Energy transport pathway in proteins: Insights from non-equilibrium molecular dynamics with elastic network model.Scientific reports · 2018Article
- Accurate PDZ/Peptide Binding Specificity with Additive and Polarizable Free Energy Simulations.Biophysical journal · 2018Article
- Convergence of Wnt, growth factor, and heterotrimeric G protein signals on the guanine nucleotide exchange factor Daple.Science signaling · 2018Article
- Phosphorylation of tight junction transmembrane proteins: Many sites, much to do.Tissue barriers · 2018Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
PDZ (PSD-95/Dlg/ZO-1) domains are protein-protein interaction modules often regulated by ligand phosphorylation. Here, we investigated the specificity, structure, and dynamics of Tiam1 PDZ domain/ligand interactions. We show that the PDZ domain specifically binds syndecan1 (SDC1), phosphorylated SDC1 (pSDC1), and SDC3 but not other syndecan isoforms. The crystal structure of the PDZ/SDC1 complex indicates that syndecan affinity is derived from amino acids beyond the four C-terminal residues. Remarkably, the crystal structure of the PDZ/pSDC1 complex reveals a binding pocket that accommodates the phosphoryl group. Methyl relaxation experiments of PDZ/SCD1 and PDZ/pSDC1 complexes reveal that PDZ-phosphoryl interactions dampen dynamic motions in a distal region of the PDZ domain by decoupling them from the ligand-binding site. Our data are consistent with a selection model by which specificity and phosphorylation regulate PDZ/syndecan interactions and signaling events. Importantly, our relaxation data demonstrate that PDZ/phospho-ligand interactions regulate protein dynamics and their coupling to distal sites.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.