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An important question in modular domain-peptide interactions, which play crucial roles in many biological processes, is how the diverse specificities exhibited by different members of a domain family are encoded in a common scaffold. Analysis of the Src homology (SH) 2 family has revealed that its specificity is determined, in large part, by the configuration of surface loops that regulate ligand access to binding pockets. In a distinct manner, SH3 domains employ loops for ligand recognition. The PDZ domain, in contrast, achieves specificity by co-evolution of binding-site residues. Thus, the conformational and sequence variability afforded by surface loops and binding sites provides a general mechanism by which to encode the wide spectrum of specificities observed for modular protein interaction domains. Copyright © 2010 Elsevier Ltd. All rights reserved.


Tomonori Kaneko, Sachdev S Sidhu, Shawn S C Li. Evolving specificity from variability for protein interaction domains. Trends in biochemical sciences. 2011 Apr;36(4):183-90

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PMID: 21227701

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