Ligand binding by TPR domains.

Protein Science : a Publication of the Protein Society
Aitziber L Cortajarena, Lynne Regan

Abstract

Tetratricopeptide repeat (TPR) domains bind specific peptide ligands and are thought to mediate protein-protein interactions in a variety of biological systems. Here we compare peptide ligand-binding by several different TPR domains. We present specific examples that demonstrate that TPR domains typically undergo little or no structural rearrangement upon ligand binding. Our data suggest that, contrary to a recent proposal, coupled folding and binding is not the common mechanism of ligand recognition by TPR domains.

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Citations

Jun 21, 2008·Journal of Biomolecular NMR·Virginia A JarymowyczMartin J Stone
Oct 17, 2012·Biomolecular NMR Assignments·Andrzej MaciejewskiWing-Yiu Choy
Apr 16, 2013·Bioorganic & Medicinal Chemistry·Margarita EisenbergGonen Ashkenasy
Dec 22, 2009·ACS Chemical Biology·Aitziber L CortajarenaLynne Regan
Sep 24, 2010·Journal of the American Chemical Society·Tijana Z GroveLynne Regan
Oct 21, 2011·Proceedings of the National Academy of Sciences of the United States of America·Ima-obong EbongCarol V Robinson
Jul 30, 2009·The Journal of Biological Chemistry·Divya TiwariVinay Kumar Nandicoori
Mar 23, 2010·Protein Engineering, Design & Selection : PEDS·Tijana Z GroveLynne Regan
Apr 19, 2013·Journal of the Royal Society, Interface·Tijana Z GroveAitziber L Cortajarena
Nov 22, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·James E TooleyR Blake Hill
May 14, 2009·HFSP Journal·Amit MorYaakov Levy
Jun 21, 2014·Nanoscale·Sara H MejíasAitziber L Cortajarena
Jan 12, 2012·Molecular BioSystems·Aleksandra Filipovska, Oliver Rackham
Feb 5, 2016·Colloids and Surfaces. B, Biointerfaces·Sara H MejiasAitziber L Cortajarena
Nov 5, 2015·Biomacromolecules·Pierre CouleaudAitziber L Cortajarena
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Apr 17, 2008·The Biochemical Journal·Stefan H MillsonChrisostomos Prodromou
Nov 17, 2016·Frontiers in Molecular Neuroscience·Marija Kojic, Brandon Wainwright

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