Transient protein-protein interactions: structural, functional, and network properties

James R Perkins; Ilhem Diboun; Benoit H Dessailly; Jon G Lees; Christine Orengo

doi:10.1016/j.str.2010.08.007

Transient protein-protein interactions: structural, functional, and network properties

Structure. 2010 Oct 13;18(10):1233-43. doi: 10.1016/j.str.2010.08.007.

Authors

James R Perkins¹, Ilhem Diboun, Benoit H Dessailly, Jon G Lees, Christine Orengo

Affiliation

¹ Department of Structural and Molecular Biology, University College of London, Gower Street, WC1E 6BT London, UK. jperkins@biochem.ucl.ac.uk

PMID: 20947012
DOI: 10.1016/j.str.2010.08.007

Abstract

Transient interactions, which involve protein interactions that are formed and broken easily, are important in many aspects of cellular function. Here we describe structural and functional properties of transient interactions between globular domains and between globular domains, short peptides, and disordered regions. The importance of posttranslational modifications in transient interactions is also considered. We review techniques used in the detection of the different types of transient protein-protein interactions. We also look at the role of transient interactions within protein-protein interaction networks and consider their contribution to different aspects of these networks.

Publication types

Review

MeSH terms

Binding Sites
Computational Biology / methods
Models, Molecular
Protein Binding
Protein Conformation
Protein Interaction Domains and Motifs*
Protein Interaction Mapping / methods*
Protein Processing, Post-Translational
Proteins / chemistry*
Proteins / metabolism

Substances

Proteins