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A frustrated binding interface for intrinsically disordered proteins.

Per Jemth1, Xin Mu, Åke Engström

  • 1From the Department of Medical Biochemistry and Microbiology, Uppsala University, SE-75123 Uppsala, Sweden.

The Journal of Biological Chemistry
|January 15, 2014
PubMed
Summary
This summary is machine-generated.

Intrinsically disordered proteins, common in eukaryotes and linked to disease, exhibit a frustrated energy landscape in their interactions. This complexity arises from their need to bind multiple partners, impacting their folding and binding dynamics.

Keywords:
Intrinsically Disordered ProteinsKineticsProtein DomainsProtein EngineeringProtein-Protein Interactions

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) are prevalent in eukaryotes and implicated in various diseases.
  • IDPs often engage in coupled binding and folding, interacting with numerous partners.

Purpose of the Study:

  • To investigate the energy landscape of binding interfaces for interacting intrinsically disordered protein domains.
  • To understand the relationship between binding affinity, energy landscape, and functional promiscuity in IDPs.

Main Methods:

  • Utilized double mutant cycles to map the energy landscape.
  • Analyzed interaction free energies at the binding interface of two disordered domains.

Main Results:

  • The energy landscape of the binding interface was found to be largely suboptimal.
  • Despite suboptimal energies, the interaction exhibited relatively high affinity.
  • These findings suggest a frustrated energy landscape for IDP interactions.

Conclusions:

  • Intrinsically disordered protein interactions are characterized by a frustrated energy landscape.
  • This frustration is likely a consequence of the functional promiscuity inherent to IDPs.
  • Understanding these landscapes is crucial for deciphering IDP function and disease association.