IMR Press / FBL / Volume 16 / Issue 4 / DOI: 10.2741/3787

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
From sequence to structural analysis in protein phosphorylation motifs
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1 Biocomputing Group, Department of Biochemical Science A Rossi Fanelli, Sapienza University of Rome, P le Aldo Moro 5, Rome, Italy
2 European Molecular Biology Laboratory, Postfach 10.2209, 69012 Heidelberg, Germany
3 Biobyte solutions GmbH, Boxbergring 16, 69126 Heidelberg, Germany
4 Center for Molecular Bioinformatics, Department of Biology, University of Rome Tor Vergata, Italy

Academic Editor: Martin Schiller

Front. Biosci. (Landmark Ed) 2011, 16(4), 1261–1275; https://doi.org/10.2741/3787
Published: 1 January 2011
(This article belongs to the Special Issue Short function motifs in proteins)
Abstract

Phosphorylation is the most widely studied post-translational modification occurring in cells. While mass spectrometry-based proteomics experiments are uncovering thousands of novel in vivo phosphorylation sites, the identification of kinase specificity rules still remains a relatively slow and often inefficacious task. In the last twenty years, many efforts have being devoted to the experimental and computational identification of sequence and structural motifs encoding kinase-substrate interaction key residues and the phosphorylated amino acid itself. In this review, we retrace the road to the discovery of phosphorylation sequence motifs, examine the progresses achieved in the detection of three-dimensional motifs and discuss their importance in the understanding of regulation and de-regulation of many cellular processes.

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