Transient protein-protein interactions: structural, functional, and network properties.
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.
Department of Structural and Molecular Biology, University College of London, Gower Street, WC1E 6BT London, UK. jperkins@biochem.ucl.ac.uk
James R
JR
Perkins
Ilhem
I
Diboun
Benoit H
BH
Dessailly
Jon G
JG
Lees
Christine
C
Orengo
D001665:Binding Sites; D019295:Computational Biology / Q000379:methods; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping / Q000379:methods*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D011506:Proteins