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Systematic investigation of protein–small molecule interactions
Author(s) -
Li Xiyan,
Wang Xin,
Snyder Michael
Publication year - 2013
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1111
Subject(s) - allosteric regulation , small molecule , protein–protein interaction , cell signaling , function (biology) , computational biology , biology , signal transduction , microbiology and biotechnology , chemistry , enzyme , biochemistry
Cell signaling is extensively wired between cellular components to sustain cell proliferation, differentiation, and adaptation. The interaction network is often manifested in how protein function is regulated through interacting with other cellular components including small molecule metabolites. While many biochemical interactions have been established as reactions between protein enzymes and their substrates and products, much less is known at the system level about how small metabolites regulate protein functions through allosteric binding. In the past decade, study of protein–small molecule interactions has been lagging behind other types of interactions. Recent technological advances have explored several high‐throughput platforms to reveal many “unexpected” protein–small molecule interactions that could have profound impact on our understanding of cell signaling. These interactions will help bridge gaps in existing regulatory loops of cell signaling and serve as new targets for medical intervention. In this review, we summarize recent advances of systematic investigation of protein–metabolite/small molecule interactions, and discuss the impact of such studies and their potential impact on both biological researches and medicine. © 2012 IUBMB Life, 65(1):2–8, 2013