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

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vol. 7 no. 347 ra98

DOI:

https://doi.org/10.1126/scisignal.2005722

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Science Signaling

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History:

Received July 21, 2014
Accepted September 24, 2014
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Copyright © 2014, American Association for the Advancement of Science

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Science Signaling: 7 (347)

Science Signaling

Vol 7, Issue 347
14 October 2014

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

By Kai-En Chen, Shu-Yu Lin, Mei-Ju Wu, Meng-Ru Ho, Abirami Santhanam, Chia-Cheng Chou, Tzu-Ching Meng, Andrew H. -J. Wang

Science Signaling14 Oct 2014 : ra98

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

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

By Kai-En Chen, Shu-Yu Lin, Mei-Ju Wu, Meng-Ru Ho, Abirami Santhanam, Chia-Cheng Chou, Tzu-Ching Meng, Andrew H. -J. Wang

Science Signaling14 Oct 2014 : ra98

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

Supplementary Materials
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