Supplementary Materials

Sci. Signal., 9 October 2012
DOI: 10.1126/scisignal.2003004
Supplementary Materials for:

Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove

Ágnes Garai, András Zeke, Gergő Gógl, Imre Törő, Ferenc Fördős, Hagen Blankenburg, Tünde Bárkai, János Varga, Anita Alexa, Dorothea Emig, Mario Albrecht, Attila Reményi*

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

This PDF file includes:

  • Fig. S1. Binding affinity measurements of MAPK–docking peptide interactions.
  • Fig. S2. Characterization of MKK6-mediated activation of p38α in vitro.
  • Fig. S3. Crystal structures of MAPK–docking peptide complexes.
  • Fig. S4. Manipulation of MAPK–D motif interaction specificity.
  • Fig. S5. Modification and design of MAPK binding specificity.
  • Fig. S6. Selected examples of sequence-specific, intrapeptide H bonds from various protein-peptide complex structures.
  • Table S1 caption
  • Table S2. Summary of the in silico D-motif search on the human proteome.
  • Table S3. Location of functionally relevant and characterized S/TP phosphorylation sites in D motif–containing MAPK substrates.
  • References (74) to (81)

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Other Supplementary Material for this manuscript includes the following:

  • Table S1 (Microsoft Excel format). Lists of MAPK binding consensus motif matching sequences in the human proteome.

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Format: Microsoft Excel

Size: 1.17 MB

Citation: Á. Garai, A. Zeke, G. Gógl, I. Törő, F. Fördős, H. Blankenburg, T. Bárkai, J. Varga, A. Alexa, D. Emig, M. Albrecht, A. Reményi, Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove. Sci. Signal. 5, ra74 (2012).

© 2012 American Association for the Advancement of Science

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