AI Article Synopsis
- The study focuses on intrinsically disordered proteins (IDPs) and how their lack of fixed structure affects their interaction with other molecules, specifically regarding dynamics during binding.
- Researchers examined two IDPs, IBB and Nup153FG, which interact with the same nuclear transport receptor (Importinβ) but use different mechanisms for binding.
- The findings reveal that the behavior of water at the interface of these protein complexes changes with binding: Nup153FG maintains water dynamics, while IBB shows a slowdown, highlighting the importance of these dynamics in biological functions like nuclear transport.
Article Abstract
The recognition of intrinsically disordered proteins (IDPs) is highly dependent on dynamics owing to the lack of structure. Here we studied the interplay between dynamics and molecular recognition in IDPs with a combination of time-resolving tools on timescales ranging from femtoseconds to nanoseconds. We interrogated conformational dynamics and surface water dynamics and its attenuation upon partner binding using two IDPs, IBB and Nup153FG, both of central relevance to the nucleocytoplasmic transport machinery. These proteins bind the same nuclear transport receptor (Importinβ) with drastically different binding mechanisms, coupled folding-binding and fuzzy complex formation, respectively. Solvent fluctuations in the dynamic interface of the Nup153FG-Importinβ fuzzy complex were largely unperturbed and slightly accelerated relative to the unbound state. In the IBB-Importinβ complex, on the other hand, substantial relative slowdown of water dynamics was seen in a more rigid interface. These results show a correlation between interfacial water dynamics and the plasticity of IDP complexes, implicating functional relevance for such differential modulation in cellular processes, including nuclear transport.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6563697 | PMC |
| http://dx.doi.org/10.1002/anie.201813354 | DOI Listing |
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