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Elucidation of the binding preferences of peptide recognition modules: SH3 and PDZ domains
Author(s) -
Teyra Joan,
Sidhu Sachdev S.,
Kim Philip M.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.05.043
Subject(s) - pdz domain , peptide , computational biology , sh3 domain , plasma protein binding , binding selectivity , protein–protein interaction , binding site , domain (mathematical analysis) , binding domain , modular design , biology , biochemistry , computer science , phosphorylation , mathematics , proto oncogene tyrosine protein kinase src , mathematical analysis , operating system
Peptide‐binding domains play a critical role in regulation of cellular processes by mediating protein interactions involved in signalling. In recent years, the development of large‐scale technologies has enabled exhaustive studies on the peptide recognition preferences for a number of peptide‐binding domain families. These efforts have provided significant insights into the binding specificities of these modular domains. Many research groups have taken advantage of this unprecedented volume of specificity data and have developed a variety of new algorithms for the prediction of binding specificities of peptide‐binding domains and for the prediction of their natural binding targets. This knowledge has also been applied to the design of synthetic peptide‐binding domains in order to rewire protein–protein interaction networks. Here, we describe how these experimental technologies have impacted on our understanding of peptide‐binding domain specificities and on the elucidation of their natural ligands. We discuss SH3 and PDZ domains as well characterized examples, and we explore the feasibility of expanding high‐throughput experiments to other peptide‐binding domains.