A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5

Yuan-Yuan Zhang, Jia-Wei Wu, Zhi-Xin Wang*

*To whom correspondence should be addressed. E-mail: zhixinwang{at}mail.tsinghua.edu.cn

This PDF file includes:

• Fig. S1. Comparison of the uncomplexed KBD^MKP5 with KBD^MKP5 from the p38α-KBD^MKP5 complex.
• Fig. S2. Comparison of the electrostatic interactions in the CD domains of p38α and ERK2.
• Fig. S3. Comparison of the complex structures of p38α-KBD^MKP5 and p38α-MK2.
• Fig. S4. Effect of KBD^MKP5 on the kinase activity of phosphorylated p38α toward different substrates.
• Fig. S5. Effect of KBD^MKP5 on the interaction of p38α with different cognate partners.
• Fig. S6. Superimposition of the four molecules within the asymmetric unit of the KBD^MKP7 structure.
• Table S1. Kinetic parameters of full-length MKP5 and its catalytic domain toward phosphorylated ERK2 or p38α.
• Table S2. Kinetic parameters of full-length MKP5 and its mutants with phosphorylated p38α as substrate.
• Table S3. Kinetic parameters of MKP7 (residues 5 to 303) and its mutants with phosphorylated p38α as substrate.
• References
  

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