Supplementary Materials

Supplementary Materials for:

Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases

Mariana Lemos Duarte, Darlene Aparecida Pena, Felipe Augusto Nunes Ferraz, Denise Aparecida Berti, Tiago José Paschoal Sobreira, Helio Miranda Costa-Junior, Munira Muhammad Abdel Baqui, Marie-Hélène Disatnik, José Xavier-Neto, Paulo Sérgio Lopes de Oliveira,* Deborah Schechtman*

*Corresponding author. E-mails: deborah{at}iq.usp.br (D.S.); paulo.oliveira{at}lnbio.org.br (P.S.L.d.O.)

This PDF file includes:

  • Fig. S1. Thr253, Lys163, and Lys164 are conserved in vertebrate α-tubulin.
  • Fig. S2. Specificity of the polyclonal antiserum recognizing α-tubulin phosphorylated on Thr253.
  • Fig. S3. Models of known PKA substrates phosphorylated within sites in linear consensus motifs.
  • Legend for table S1
  • Table S2. RMSD calculation for PKA-docked models with linear consensus motifs, compared to the linear peptide and the nondocked substrate model.

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Technical Details

Format: Adobe Acrobat PDF

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Other Supplementary Material for this manuscript includes the following:

  • Table S1 (Microsoft Excel format). Substrates of PKA obtained from PhosphositePlus modeled through homology modeling.
  • Models S1. PDB files of the models of the three substrates with linear consensus motifs, three substrates with structurally formed consensus motifs, and the α-tubulin–PKC complex.

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[Download Model S1]


Citation: M. L. Duarte, D. A. Pena, F. A. N. Ferraz, D. A. Berti, T. J. P. Sobreira, H. M. Costa-Junior, M. M. A. Baqui, M.-H. Disatnik, J. Xavier-Neto, P. S. L. de Oliveira, D. Schechtman, Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases. Sci. Signal. 7, ra105 (2014).

© 2014 American Association for the Advancement of Science