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Sci. Signal., 2 March 2010
[DOI: 10.1126/scisignal.2000525]

Supplementary Materials for:

Crystal Structure of the α-Kinase Domain of Dictyostelium Myosin Heavy Chain Kinase A

Qilu Ye, Scott W. Crawley, Yidai Yang, Graham P. Côté,* Zongchao Jia

*To whom correspondence should be addressed. E-mail: coteg{at}

This PDF file includes:

  • Fig. S1. Alignment of the sequences of multiple α-kinase domains.
  • Fig. S2. Evolutionary relationships of the α-kinases.
  • Fig. S3. The ATP-ADP exchange reaction catalyzed by A-CAT.
  • Fig. S4. Comparison of the active sites of A-CAT and TRPM7-CAT.
  • Fig. S5. Docking of a Thr-Lys dipeptide into the active-site pocket of the A-CAT–ADP complex.
  • Table S1. Interaction distances for the relevant ions and water molecules in the various A-CAT complexes.
  • Table S2. Conservation of functionally important residues in the α-kinase domain.
  • Table S3. Summary of the missing residues in the structures of A-CAT and A-CAT-D766A.
  • Table S4. α-Kinase domains included in the multiple sequence alignment.
  • References

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Technical Details

Format: Adobe Acrobat PDF

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Citation: Q.Ye, S. W. Crawley, Y. Yang, G. P. Côté, Z. Jia, Crystal structure of the α-kinase domain of Dictyostelium myosin heavy chain kinase A. Sci. Signal. 3, ra17 (2010).

© 2010 American Association for the Advancement of Science

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