作者: Gerd Kock , Markus Dicks , Rolf Heumann , Kai S. Erdmann , Raphael Stoll
DOI: 10.1007/S12104-010-9242-9
关键词: Protein tyrosine phosphatase 、 Scaffold protein 、 PDZ domain 、 Protein domain 、 Computational biology 、 Domain (software engineering) 、 Peptide sequence 、 Biochemistry 、 SH2 domain 、 PTPN13 、 Chemistry 、 Structural biology
摘要: 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 extended PDZ3 PTP-BL. These provide basis for detailed structural investigation interaction between domains PTP-BL well their with ligands. It will lead to better understanding proposed function these in multi-protein complexes assembled by PTB-BL.