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Structural and dynamical aspects of evolutionarily conserved protein-protein complexes

Tandon, H and Vishwanath, S and Srinivasan, N (2020) Structural and dynamical aspects of evolutionarily conserved protein-protein complexes. [Book Chapter]

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Official URL: https://doi.org/10.1142/9789811211874_0001

Abstract

Proteins interact with other proteins to perform vital cellular functions. Understanding various features of protein-protein interfaces is important for their prediction as well as designing inhibitors/activators of protein-protein interactions (PPIs). In this article, the structural and dynamical characteristics of PPIs and their evolutionary conservation have been reviewed. The extent of partner retention and similarity in the quaternary structure and quaternary states of protein-protein complexes (PPCs) depends on the evolutionary divergence among related proteins. Similar interacting modes are observed in protein complexes if the related proteins share high sequence identity, and at low sequence identities, interface residues may differ. Presence of additional structural elements also brings diversity among the evolutionarily related PPCs. These observations suggest caution when predicting interfaces based on homologous complexes with low sequence identities. Binding of two proteins can also lead to change in structure and/or dynamics at the interfaces as well as distant sites in PPCs. These changes often have functional relevance and regulate protein (dis)assembly through allosteric communication. Various examples have been discussed in this article to understand how sequence identities between evolutionarily conserved PPCs affect their interfacial characteristics and how the binding of partner proteins affects their structure and dynamics. © 2020 by World Scientific Publishing Co. Pte. Ltd.

Item Type: Book Chapter
Publication: Protein Interactions: Computational Methods, Analysis And Applications
Publisher: World Scientific Publishing Co.
Additional Information: The copyright for this article belongs to World Scientific Publishing Co.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 28 Nov 2021 09:56
Last Modified: 28 Nov 2021 09:56
URI: http://eprints.iisc.ac.in/id/eprint/70323

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