Uncovering new aspects of protein interactions through analysis of specificity landscapes in peptide recognition domains
Open Access
- 3 April 2012
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 586 (17) , 2764-2772
- https://doi.org/10.1016/j.febslet.2012.03.054
Abstract
Protein interactions underlie all biological processes. An important class of protein interactions, often observed in signaling pathways, consists of peptide recognition domains binding short protein segments on the surface of their target proteins. Recent developments in experimental techniques have uncovered many such interactions and shed new lights on their specificity. To analyze these data, novel computational methods have been introduced that can accurately describe the specificity landscape of peptide recognition domains and predict new interactions. Combining large‐scale analysis of binding specificity data with structure‐based modeling can further reveal new biological insights into the molecular recognition events underlying signaling pathways.Keywords
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