ArticleInternational journal of molecular sciences2011
Anchoring intrinsically disordered proteins to multiple targets: lessons from N-terminus of the p53 protein.
Article in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Structural investigation of CDCA3-Cdh1 protein-protein interactions using in vitro studies and molecular dynamics simulation.Protein science : a publication of the Protein Society · 2023Article
- Anchor Residues Govern Binding and Folding of an Intrinsically Disordered Domain.ACS chemical biology · 2022Article
- Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies.International journal of molecular sciences · 2019Review
- Binding cavities and druggability of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2015Article
- Advantages of proteins being disordered.Protein science : a publication of the Protein Society · 2014Review
- Molecular dynamics of the full-length p53 monomer.Cell cycle (Georgetown, Tex.) · 2013Article
- Inherent relationships among different biophysical prediction methods for intrinsically disordered proteins.Biophysical journal · 2013Article
- Ligand clouds around protein clouds: a scenario of ligand binding with intrinsically disordered proteins.PLoS computational biology · 2013Article
- Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics study.PLoS computational biology · 2012Article
- A preformed binding interface in the unbound ensemble of an intrinsically disordered protein: evidence from molecular simulations.PLoS computational biology · 2012Article
- Binding free energy landscape of domain-peptide interactions.PLoS computational biology · 2011Article
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2 authors.
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Abstract
Anchor residues, which are deeply buried upon binding, play an important role in protein-protein interactions by providing recognition specificity and facilitating the binding kinetics. Up to now, studies on anchor residues have been focused mainly on ordered proteins. In this study, we investigated anchor residues in intrinsically disordered proteins (IDPs) which are flexible in the free state. We identified the anchor residues of the N-terminus of the p53 protein (Glu17-Asn29, abbreviated as p53N) which are involved in binding with two different targets (MDM2 and Taz2), and analyzed their side chain conformations in the unbound states. The anchor residues in the unbound p53N were found to frequently sample conformations similar to those observed in the bound complexes (i.e., Phe19, Trp23, and Leu26 in the p53N-MDM2 complex, and Leu22 in the p53N-Taz2 complex). We argue that the bound-like conformations of the anchor residues in the unbound state are important for controlling the specific interactions between IDPs and their targets. Further, we propose a mechanism to account for the binding promiscuity of IDPs in terms of anchor residues and molecular recognition features (MoRFs).
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