Sequence-specific 1H, 13C, and 15N assignment of the extended PDZ3 domain of the protein tyrosine phosphatase basophil-like PTP-BL.
Protein tyrosine phosphatase basophil-like (PTP-BL), also known as PTPN13, represents a large multi domain non-transmembrane scaffolding protein that contains five PDZ domains. Here we report the complete resonance assignments of the extended PDZ3 domain of PTP-BL. These assignments provide a basis for the detailed structural investigation of the interaction between the PDZ domains of PTP-BL as well as of their interaction with ligands. It will also lead to a better understanding of the proposed scaffolding function of these domains in multi-protein complexes assembled by PTB-BL.
Kock
Gerd
G
Biomolecular NMR, Faculty of Chemistry and Biochemistry, Ruhr-University of Bochum, 44780, Bochum, Germany. gerd.kock@rub.de
Dicks
Markus
M
Heumann
Rolf
R
Erdmann
Kai S
KS
Stoll
Raphael
R
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D006859:Hydrogen; D051379:Mice; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D054731:PDZ Domains; D054595:Protein Tyrosine Phosphatase, Non-Receptor Type 13 / Q000737:chemistry*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D054595:Protein Tyrosine Phosphatase, Non-Receptor Type 13