Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain–modulated complex formation-Reference-Cited by-同舟云学术

Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain–modulated complex formation

Author:

Chen Kai-En¹,Lin Shu-Yu¹,Wu Mei-Ju¹,Ho Meng-Ru¹,Santhanam Abirami¹,Chou Chia-Cheng¹²,Meng Tzu-Ching¹³,-J. Wang Andrew H.¹²³⁴

Affiliation:

1. Institute of Biological Chemistry, Academia Sinica, Taipei 11581, Taiwan.

2. National Core Facility for Protein Structural Analysis, Academia Sinica, Taipei 11581, Taiwan.

3. Institute of Biochemical Sciences, National Taiwan University, Taipei 10717, Taiwan.

4. Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, Taipei 11047, Taiwan.

Abstract

Structural analysis of a phosphatase-kinase complex defines a role for the PDZ domain in regulating kinase inactivation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference70 articles.

Cited by 26 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献