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Sci. Signal., 20 December 2011
[DOI: 10.1126/scisignal.2002241]

Supplementary Materials for:

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 KBDMKP5 with KBDMKP5 from the p38α-KBDMKP5 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-KBDMKP5 and p38α-MK2.
  • Fig. S4. Effect of KBDMKP5 on the kinase activity of phosphorylated p38α toward different substrates.
  • Fig. S5. Effect of KBDMKP5 on the interaction of p38α with different cognate partners.
  • Fig. S6. Superimposition of the four molecules within the asymmetric unit of the KBDMKP7 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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Citation: Y.-Y. Zhang, J.-W. Wu, Z.-X. Wang, A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5. Sci. Signal. 4, ra88 (2011).

© 2011 American Association for the Advancement of Science


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