title: Sequence-specific backbone ¹H, ¹³C and ¹⁵N assignments of the 34 kDa catalytic domain of PTPN5 (STEP).
abstract: PTPN5 is a protein tyrosine phosphatase that plays an integral role in regulating excitatory postsynaptic activity. The sequence-specific backbone assignments of the murine PTPN5 catalytic domain have been determined based on triple-resonance experiments using uniformly [(2)H,(13)C,(15)N]-labeled protein.
authors: Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI, 02903, USA.
authors: Dana M
authors: DM
authors: Francis
authors: Rebecca
authors: R
authors: Page
authors: Wolfgang
authors: W
authors: Peti
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D020134:Catalytic Domain; D006859:Hydrogen; D051379:Mice; D008970:Molecular Weight; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D054558:Protein Tyrosine Phosphatases, Non-Receptor / Q000737:chemistry*
chemical_list: D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D054558:Protein Tyrosine Phosphatases, Non-Receptor; C082101:Ptpn5 protein, mouse