Bryan T Martin, Michael W Clarkson, Ping Wu, Paola Di Lello
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引用次数: 0
Abstract
Protein Tyrosine Phosphatase Non-receptor type 22 (PTPN22) is a tyrosine-phosphatase that plays a major role in inhibiting T-cell activation in immune cells. Recent studies have revealed that downregulation of PTPN22 triggers T-cell activation and enhances antitumor immune response, thereby identifying PTPN22 as a potential pharmacological target in cancer-immunology.Here we report the 1H, 15N and 13C backbone resonance assignment for the 35.6 kDa catalytic domain of human PTPN22. This assignment will provide an essential experimental tool to identify and characterize potential PTPN22 inhibitors.
期刊介绍:
Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties.
Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.