IMR Press / FBL / Volume 14 / Issue 3 / DOI: 10.2741/3292

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
SH2 domain binding to phosphopeptide ligands: potential for drug targeting
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1 Section of Infectious Disease, Department of Medicine, Baylor College of Medicine, One Baylor Plaza, Houston, TX., 77030, USA
2 Department of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX., 77030, USA
Academic Editor:Martin Schiller
Front. Biosci. (Landmark Ed) 2009, 14(3), 1010–1022; https://doi.org/10.2741/3292
Published: 1 January 2009
(This article belongs to the Special Issue Short function motifs in proteins)
Abstract

SH2 domains are modular components of a wide range of functionally diverse proteins involved in mammalian signal transduction including enzymes, adaptors, regulators and transcription factors. Members of the SH2 domain family recognize a wide variety of short tyrosine phosphorylated peptide motifs. Biochemical and structural studies have revealed key aspects of these interactions that account for their ability to discriminate between different sequence motifs. While the mechanism of phosphotyrosine (pTyr) recognition is remarkably conserved among the SH2 domains, differences in recognition of phosphopeptide residues N and especially C-terminal to the pTyr have been identified that contribute to selectivity. The basis for SH2- phosphopeptide recognition is discussed in light of the available structural and biochemical data with a focus on recent information regarding SH2 domains within a new class found within the signal transducer and activator of transcription (STAT) protein family.

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