The binding affinity of PTPN13’s tandem PDZ2/3 domain is allosterically modulated

The binding affinity of PTPN13’s tandem PDZ2/3 domain is allosterically modulated

Abstract Background Protein tyrosine phosphatase PTPN13, also known as PTP-BL in mice, is a large multi-domain non-transmembrane scaffolding protein with a molecular mass of 270 kDa. It is involved in the regulation of several cellular processes such as cytokinesis and actin-cytoskeletal rearrangeme...

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Bibliographic Details
Main Authors: Markus Dicks, Gerd Kock, Bastian Kohl, Xueyin Zhong, Stefanie Pütz, Rolf Heumann, Kai S. Erdmann, Raphael Stoll
Format: Article
Language:English
Published: BMC 2019-07-01
Series:BMC Molecular and Cell Biology
Subjects:
PTPN13
APC
PDZ2/3 tandem domain
NMR
Allosteric affinity modulation
Online Access:http://link.springer.com/article/10.1186/s12860-019-0203-6

Internet

http://link.springer.com/article/10.1186/s12860-019-0203-6

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