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Uncovering new aspects of protein interactions through analysis of specificity landscapes in peptide recognition domains
Author(s) -
Gfeller David
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.2012.03.054
Subject(s) - computational biology , protein–protein interaction , molecular recognition , peptide , biology , chemistry , microbiology and biotechnology , biochemistry , organic chemistry , molecule
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.