Protein-Protein Interactions and Prediction: A Comprehensive Overview

被引:0
|
作者
Sowmya, Gopichandran [1 ,2 ]
Ranganathan, Shoba [1 ,2 ]
机构
[1] Macquarie Univ, Dept Chem & Biomol Sci, Sydney, NSW 2109, Australia
[2] Macquarie Univ, ARC Ctr Excellence Bioinformat, Sydney, NSW 2109, Australia
来源
PROTEIN AND PEPTIDE LETTERS | 2014年 / 21卷 / 08期
关键词
Binding sites; interface features; prediction; protein complexes; protein-protein interactions; HOT-SPOTS; SUBUNIT INTERFACES; BINDING-SITES; STRUCTURAL CLASSIFICATION; CONFORMATIONAL-CHANGE; INTERACTION DATABASE; COMPLEXES; RESIDUES; DOCKING; RECOGNITION;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Molecular function in cellular processes is governed by protein-protein interactions (PPIs) within biological networks. Selective yet specific association of these protein partners contributes to diverse functionality such as catalysis, regulation, assembly, immunity, and inhibition in a cell. Therefore, understanding the principles of protein-protein association has been of immense interest for several decades. We provide an overview of the experimental methods used to determine PPIs and the key databases archiving this information. Structural and functional information of existing protein complexes confers knowledge on the principles of PPI, based on which a classification scheme for PPIs is then introduced. Obtaining high-quality non-redundant datasets of protein complexes for interaction characterisation is an essential step towards deciphering their underlying binding principles. Analysis of physicochemical features and their documentation has enhanced our understanding of the molecular basis of protein-protein association. We describe the diverse datasets created/collected by various groups and their key findings inferring distinguishing features. The currently available interface databases and prediction servers have also been compiled.
引用
收藏
页码:779 / 789
页数:11
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