NEW EMBO MEMBER’S REVIEW: Diversity of protein–protein interactions
AUTOR(ES)
Nooren, Irene M.A.
FONTE
Oxford University Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=165629Documentos Relacionados
- NEW EMBO MEMBER’S REVIEW: Hsp70 interactions with the p53 tumour suppressor protein
- NEW EMBO MEMBER’S REVIEW: Addressing protein localization within the nucleus
- NEW EMBO MEMBER’S REVIEW: Addressing protein localization within the nucleus
- NEW EMBO MEMBER’S REVIEW: Functional aspects of protein mono-ADP-ribosylation
- NEW EMBO MEMBER’S REVIEW: The importance of aquaporin water channel protein structures
