A number of studies have addressed the question of which are the critical residues at protein-binding sites. These studies examined either a single or a few protein-protein interfaces. The most extensive study to date has been an analysis of alanine-scanning mutagenesis. However, although the total
Charged residues at protein interaction interfaces: Unexpected conservation and orchestrated divergence
β Scribed by Nan Zhao; Bin Pang; Chi-Ren Shyu; Dmitry Korkin
- Book ID
- 105356661
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2011
- Tongue
- English
- Weight
- 421 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0961-8368
- DOI
- 10.1002/pro.655
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β¦ Synopsis
Abstract
Proteinβprotein interactions play an essential role in the functioning of cell. The importance of charged residues and their diverse role in proteinβprotein interactions have been well studied using experimental and computational methods. Often, charged residues located in protein interaction interfaces are conserved across the families of homologous proteins and protein complexes. However, on a large scale, it has been recently shown that charged residues are significantly less conserved than other residue types in protein interaction interfaces. The goal of this work is to understand the role of charged residues in the protein interaction interfaces through their conservation patterns. Here, we propose a simple approach where the structural conservation of the charged residue pairs is analyzed among the pairs of homologous binary complexes. Specifically, we determine a large set of homologous interactions using an interaction interface similarity measure and catalog the basic types of conservation patterns among the charged residue pairs. We find an unexpected conservation pattern, which we call the correlated reappearance, occurring among the pairs of homologous interfaces more frequently than the fully conserved pairs of charged residues. Furthermore, the analysis of the conservation patterns across different superkingdoms as well as structural classes of proteins has revealed that the correlated reappearance of charged residues is by far the most prevalent conservation pattern, often occurring more frequently than the unconserved charged residues. We discuss a possible role that the new conservation pattern may play in the longβrange electrostatic steering effect.
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