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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...

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Targeting Nipah virus replication: A fluorescence polarization assay for high-throughput modulators screening against the N<sub>TAIL</sub>-XD interaction.

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Updated: May 10, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Dissecting partner recognition by an intrinsically disordered protein using descriptive random mutagenesis.

Antoine Gruet1, Marion Dosnon, Andrea Vassena

  • 1CNRS and Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, UMR 7257, 13288 Marseille, France.

Journal of Molecular Biology
|July 2, 2013
PubMed
Summary

Descriptive random mutagenesis (DRM) reveals key insights into intrinsically disordered protein (IDP) interactions. This method identified new binding determinants and regulatory sites for the measles virus nucleoprotein C-terminal domain (NTAIL) and its partner X domain (XD).

Keywords:
DRMGFPIDPIntrinsically disordered proteinMeVMoREdescriptive random mutagenesisgreen fluorescent proteinlibrarymeasles virusmolecular recognition elementpartner recognitionprotein complementation assayprotein–protein interactionssplit-GFP reassembly

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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

  • Molecular biology
  • Virology
  • Protein-protein interactions

Background:

  • Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes, but their dynamic nature complicates the study of their binding interactions.
  • Understanding the molecular determinants governing the binding efficiency of IDPs is essential for deciphering their functions and developing targeted therapeutics.
  • The interaction between the measles virus nucleoprotein C-terminal domain (NTAIL) and the viral phosphoprotein X domain (XD) serves as a model system for studying IDP binding.

Purpose of the Study:

  • To gain insights into the molecular determinants of binding efficiency in intrinsically disordered proteins (IDPs).
  • To characterize the effects of random amino acid substitutions in NTAIL on its interaction with XD.
  • To introduce and validate a novel mutagenesis approach termed 'descriptive random mutagenesis' (DRM) for studying IDP interactions.

Main Methods:

  • Descriptive random mutagenesis (DRM) using error-prone PCR to generate random NTAIL variants.
  • Random selection of NTAIL variants without any selection pressure.
  • Characterization of variant sequences and their binding abilities toward XD.

Main Results:

  • DRM identified known and novel determinants of the NTAIL/XD interaction.
  • The primary interaction site of NTAIL was found to be poorly evolvable regarding binding efficiency.
  • A critical NTAIL residue stabilizing the NTAIL/XD complex and regulatory sites dampening the interaction were discovered.

Conclusions:

  • Descriptive random mutagenesis (DRM) is a valuable approach for studying the binding abilities of intrinsically disordered proteins (IDPs).
  • The study provides new insights into the NTAIL/XD interaction, highlighting the evolvability constraints of primary interaction sites and the role of regulatory sites.
  • DRM offers a complementary strategy to directed evolution for understanding protein-protein interactions involving IDPs.