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Transient association between proteins elicits alteration of dynamics at sites far away from interfaces

Abstract : Proteins are known to undergo structural changes upon binding to partner proteins. But the prevalence, extent, location, and function of change in protein dynamics due to transient protein-protein interactions is not well-documented. Here, we have analysed a dataset of 58 protein-protein complexes of known 3-D structure and structures of their corresponding unbound forms to evaluate dynamics changes induced by binding. 55% cases showed significant dynamics change away from the interfaces. This change is not always accompanied by an observed structural change. Binding of protein partner is found to alter inter-residue communication within the tertiary structure for about 90% cases. Also, residue motions accessible to proteins in unbound form were not always maintained in the bound form. Further analyses revealed functional roles for the distant site where dynamics change was observed. Overall, results presented here strongly suggest that alteration of protein dynamics due to binding of a partner protein commonly occurs.
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https://www.hal.inserm.fr/inserm-03543689
Contributor : Alexandre G. de Brevern Connect in order to contact the contributor
Submitted on : Wednesday, January 26, 2022 - 10:55:21 AM
Last modification on : Friday, August 5, 2022 - 12:01:02 PM
Long-term archiving on: : Wednesday, April 27, 2022 - 6:33:48 PM

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Himani Tandon, Alexandre de Brevern, Narayanaswamy Srinivasan. Transient association between proteins elicits alteration of dynamics at sites far away from interfaces. Structure, Elsevier (Cell Press), 2021, 29 (4), pp.371-384.e3. ⟨10.1016/j.str.2020.11.015⟩. ⟨inserm-03543689⟩

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