All proteins require physical interactions with other proteins in order to perform their functions. Most of them oligomerize into homomers, and a vast majority of these homomers interact with other proteins, at least part of the time, forming transient or obligate heteromers. In the present paper, we review the structural, biophysical and evolutionary aspects of these protein interactions. We discuss how protein function and stability benefit from oligomerization, as well as evolutionary pathways by which oligomers emerge, mostly from the perspective of homomers. Finally, we emphasize the specificities of heteromeric complexes and their structure and evolution. We also discuss two analytical approaches increasingly being used to study protein structures as well as their interactions. First, we review the use of the biological networks and graph theory for analysis of protein interactions and structure. Secondly, we discuss recent advances in techniques for detecting correlated mutations, with the emphasis on their role in identifying pathways of allosteric communication.
The emergence of protein complexes: quaternary structure, dynamics and allostery
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Tina Perica, Joseph A. Marsh, Filipa L. Sousa, Eviatar Natan, Lucy J. Colwell, Sebastian E. Ahnert, Sarah A. Teichmann; The emergence of protein complexes: quaternary structure, dynamics and allostery. Biochem Soc Trans 1 June 2012; 40 (3): 475–491. doi: https://doi.org/10.1042/BST20120056
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