1. Sequence-specific 1H, 13C, and 15N assignment of the extended PDZ3 domain of the protein tyrosine phosphatase basophil-like PTP-BL
- Author
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Markus Dicks, Gerd Kock, Kai S. Erdmann, Raphael Stoll, and Rolf Heumann
- Subjects
Scaffold protein ,Carbon Isotopes ,animal structures ,Nitrogen Isotopes ,Chemistry ,Protein domain ,PDZ domain ,Protein Tyrosine Phosphatase, Non-Receptor Type 13 ,PDZ Domains ,Protein tyrosine phosphatase ,Computational biology ,SH2 domain ,environment and public health ,Biochemistry ,Domain (software engineering) ,Mice ,enzymes and coenzymes (carbohydrates) ,PTPN13 ,Structural Biology ,Animals ,Amino Acid Sequence ,Nuclear Magnetic Resonance, Biomolecular ,Peptide sequence ,Hydrogen - Abstract
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.
- Published
- 2010