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Protein Interaction Energy Landscapes are Shaped by Functional and also Non-functional Partners.

Abstract：

:In the crowded cell, a strong selective pressure operates on the proteome to limit the competition between functional and non-functional protein-protein interactions. We developed an original theoretical framework in order to interrogate how this competition constrains the behavior of proteins with respect to their partners or random encounters. Our theoretical framework relies on a two-dimensional (2D) representation of interaction energy landscapes, with 2D energy maps, which reflect in a synthetic way the spatial distribution of the interaction propensity of a protein surface for another protein. We realized the interaction propensity mapping of proteins' surfaces in interaction with functional and arbitrary partners and asked whether the distribution of their interaction propensity is conserved during evolution. Therefore, we performed several thousands of cross-docking simulations to systematically characterize the energy landscapes of 103 proteins interacting with different sets of homologs, corresponding to their functional partner's family or arbitrary protein families. Then, we systematically compared the energy maps resulting from the docking of each protein with the different protein families of the dataset. Strikingly, we show that the interaction propensity not only of the binding sites but also of the rest of the surface is conserved for docking partners belonging to the same protein family. Interestingly, this observation holds for docked proteins corresponding to true but also arbitrary partners. Our theoretical framework enables the characterization of the energy behavior of a protein in interaction with hundreds of proteins and opens the way for the characterization of the behavior of proteins in a specific environment.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Schweke H,Mucchielli MH,Sacquin-Mora S,Bei W,Lopes A

doi

10.1016/j.jmb.2019.12.047

subject

Has Abstract

pub_date

2020-02-14 00:00:00

pages

1183-1198

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(20)30033-4

journal_volume

432

pub_type

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