title: Diversity of protein-protein interactions.
abstract: In this review, we discuss the structural and functional diversity of protein-protein interactions (PPIs) based primarily on protein families for which three-dimensional structural data are available. PPIs play diverse roles in biology and differ based on the composition, affinity and whether the association is permanent or transient. In vivo, the protomer's localization, concentration and local environment can affect the interaction between protomers and are vital to control the composition and oligomeric state of protein complexes. Since a change in quaternary state is often coupled with biological function or activity, transient PPIs are important biological regulators. Structural characteristics of different types of PPIs are discussed and related to their physiological function, specificity and evolution.
authors.affiliation: European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
authors.forename: Irene M A
authors.initials: IM
authors.lastname: Nooren
authors.forename: Janet M
authors.initials: JM
authors.lastname: Thornton
mesh_terms: D000818:Animals; D019281:Dimerization; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D021122:Protein Subunits; D011506:Proteins