Structural and kinetic characterization of DUSP5 with a Di-phosphorylated tripeptide substrate from the ERK activation loop
These studies indicate a preference for pY before pT binding, but with ability to bind and dephosphorylate both residues, and with a dynamic active site pocket that accommodates multiple tripeptide orientations.
Authors
- Marat R. Talipov (ORCID: https://orcid.org/0000-0002-7559-9666)
- Ankan Gupta (ORCID: https://orcid.org/0000-0003-0111-6294)
- Noreena L. Sweeney
- Debbie C. Crans (ORCID: https://orcid.org/0000-0001-7792-3450)
- Raulia Syrlybaeva
- Ramani Ramchandran (ORCID: https://orcid.org/0000-0002-3555-6119)
- Andrea Imhoff
- Robert D. Bongard
- Daniel S. Sem (ORCID: https://orcid.org/0000-0002-2108-6646)
- Edgar Del Carpio (ORCID: https://orcid.org/0000-0001-7358-6178)
- Costanza Garcia-Keller
Institutions
- New Mexico State University (US)
- Concordia University Wisconsin (US)
- University of Wisconsin System (US)
- Medical College of Wisconsin (US)
- Colorado State University (US)
Publication Details
- Journal
- Frontiers in Chemical Biology
- Published
- 2024-08-05
- DOI
- https://doi.org/10.3389/fchbi.2024.1385560
- Citations
- 8
- Primary Topic
- Protein Tyrosine Phosphatases
- Type
- article
- Field-Weighted Citation Impact
- 1.87
Funders
- Children’s Hospital of Wisconsin Research Institute
- National Institutes of Health
- National Institute of General Medical Sciences