Jardin C, Sticht H (2012)
Publication Type: Journal article
Publication year: 2012
Book Volume: 29
Pages Range: 777-92
Journal Issue: 4
DOI: 10.1080/07391102.2012.10507413
Inactivation of signal transducers and activators of transcription (STAT) proteins is regulated by dual-specificity phosphatases (DSPs) with high substrate specificity. Although experiments have provided useful information about the phosphatase activity and the specificity for STATs, there is up-to-date no data at a molecular level to explain the specific recognition of STAT substrates by this subfamily of phosphatases. Here, a combined approach of molecular modeling, docking and molecular dynamics simulations was used to address the binding between DSPs and their STAT substrates. We identified a binding interface at the protein tyrosine phosphatase (PTP) domain of the DSP VHR that interacts with the SH2-domain of STAT5. This finding is consistent with previous mutational data and supports a "two-step" mechanism for the dephosphorylation event. Application of the same approach suggests the presence of a similar interface between the viral DSP VH1 and STAT1. Furthermore, the interaction network at this interface provides an explanation for the specificity of the DSP-STAT recognition.
APA:
Jardin, C., & Sticht, H. (2012). Identification of the structural features that mediate binding specificity in the recognition of STAT proteins by dual-specificity phosphatases. Journal of Biomolecular Structure & Dynamics, 29(4), 777-92. https://doi.org/10.1080/07391102.2012.10507413
MLA:
Jardin, Christophe, and Heinrich Sticht. "Identification of the structural features that mediate binding specificity in the recognition of STAT proteins by dual-specificity phosphatases." Journal of Biomolecular Structure & Dynamics 29.4 (2012): 777-92.
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