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Specificity and stability of transient protein-protein interactions

Vishwanath, Sneha and Sukhwal, Anshul and Sowdhamini, Ramanathan and Srinivasan, Narayanaswamy (2017) Specificity and stability of transient protein-protein interactions. In: CURRENT OPINION IN STRUCTURAL BIOLOGY, 44 . pp. 77-86.

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Official URL: https://doi.org/10.1016/j.sbi.2016.12.010


Remarkable features that are achieved in a protein-protein complex to precise levels are stability and specificity. Deviation from the normal levels of specificity and stability, which is often caused by mutations, could result in disease conditions. Chemical nature, 3-D arrangement and dynamics of interface residues code for both specificity and stability. This article reviews roles of interfacial residues in transient protein-protein complexes. It is proposed that aside from hotspot residues conferring stability to the complex, a small set of `rigid' residues at the interface that maintain conformation between complexed and uncomplexed forms, play a major role in conferring specificity. Exceptionally, `super hotspot' residues, which confer both stability and specificity, are attractive sites for interaction with small molecule inhibitors.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the CURRENT BIOLOGY LTD, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 01 Sep 2017 10:17
Last Modified: 01 Sep 2017 10:17
URI: http://eprints.iisc.ac.in/id/eprint/57732

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