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Diversity of Protein-protein Interactions

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Journal EMBO J
Date 2003 Jul 11
PMID 12853464
Citations 298
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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.

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References
1.
Brooijmans N, Sharp K, Kuntz I . Stability of macromolecular complexes. Proteins. 2002; 48(4):645-53. DOI: 10.1002/prot.10139. View

2.
Sintchak M, Arjara G, Kellogg B, Stubbe J, Drennan C . The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer. Nat Struct Biol. 2002; 9(4):293-300. DOI: 10.1038/nsb774. View

3.
Chothia C, Janin J . Principles of protein-protein recognition. Nature. 1975; 256(5520):705-8. DOI: 10.1038/256705a0. View

4.
Faust P, Kornfeld S, Chirgwin J . Cloning and sequence analysis of cDNA for human cathepsin D. Proc Natl Acad Sci U S A. 1985; 82(15):4910-4. PMC: 390467. DOI: 10.1073/pnas.82.15.4910. View

5.
Miller S, Lesk A, Janin J, Chothia C . The accessible surface area and stability of oligomeric proteins. Nature. 1987; 328(6133):834-6. DOI: 10.1038/328834a0. View