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The sequence-ensemble relationship in fuzzy protein complexes.

San Hadži1,2, Remy Loris3,4, Jurij Lah1

  • 1Department of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia; san.hadzi@fkkt.uni-lj.si jurij.lah@fkkt.uni-lj.si.

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|September 10, 2021
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Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) form fuzzy complexes with targets. A new model reveals that IDP sequence and interaction hotspots dictate bound states, explaining disorder in protein binding.

Keywords:
IDPallosteryfuzzy complexesintrinsic disorderprotein binding

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) interact with globular proteins, forming dynamic and structurally heterogeneous "fuzzy complexes."
  • Understanding how IDP sequence dictates their unbound ensemble is established, but the factors shaping their bound states remain unclear.

Purpose of the Study:

  • To elucidate the sequence-based determinants of IDP structural ensembles when bound to target proteins.
  • To develop a model explaining the heterogeneity observed in fuzzy complexes.

Main Methods:

  • Utilized a statistical thermodynamic model.
  • Integrated IDP sequence information with the distribution of IDP-target interaction hotspots.
  • Validated the model against NMR relaxation data and mutation-induced changes in affinity and helicity.

Main Results:

  • Demonstrated that a combination of IDP sequence and interaction hotspot distribution governs target-bound IDP ensembles.
  • The model successfully reproduces experimental dynamics, binding affinity changes, and helicity alterations upon mutation.
  • Showcased how target-bound IDP ensembles adapt to mutations to balance conformational freedom and interaction energy.

Conclusions:

  • Established a sequence-ensemble relationship for fuzzy complexes, explaining IDP disorder in folding-upon-binding.
  • The findings provide a framework for understanding how IDPs achieve functional diversity through adaptable structural ensembles.
  • This work deepens the comprehension of intrinsically disordered protein interactions and their role in biological regulation.