| Identification of the Structural Features that Mediate Binding Specificity in the Recognition of STAT Proteins by Dual-Specificity Phosphatases. | |
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MedLine Citation:
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PMID: 22208278 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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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. |
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Authors:
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C Jardin; F R Salsbury |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of biomolecular structure & dynamics Volume: 29 ISSN: 1538-0254 ISO Abbreviation: J. Biomol. Struct. Dyn. Publication Date: 2012 Feb |
Date Detail:
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Created Date: 2012-01-02 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8404176 Medline TA: J Biomol Struct Dyn Country: United States |
Other Details:
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Languages: eng Pagination: 777-92 Citation Subset: IM |
Affiliation:
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Institute for Biochemistry, Universitat Erlangen-Nurnberg, Fahrstrasse 17, 91054 Erlangen, Germany. Christophe.Jardin@biochem.uni-erlangen.de. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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