Open Access
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From sequence to structural analysis in protein phosphorylation motifs
Allegra Via1,Francesca Diella1,Toby James Gibson1,Manuela Helmer-Citterich1
1
Biocomputing Group, Department of Biochemical Science A Rossi Fanelli, Sapienza University of Rome, P le Aldo Moro 5, Rome, Italy
DOI: 10.2741/3787 Volume 16 Issue 4, pp.1261-1275
Published: 01 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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Allegra Via, Francesca Diella, Toby James Gibson, Manuela Helmer-Citterich. From sequence to structural analysis in protein phosphorylation motifs. Frontiers in Bioscience-Landmark. 2011. 16(4); 1261-1275.