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. 2019 Nov 29;39(1):e102406. doi: 10.15252/embj.2019102406

Figure EV3. Structural analysis of the identified 9‐amino acid sequence. (This figure is related to Fig 2 and Appendix Fig S3).

Figure EV3

  1. Illustration of the identified 9‐amino acid residues in the average YAP‐WW1/SMAD7‐PY structure. The initial structure was derived from NMR solution structure (2LTW). SMAD7‐PY peptide was adjusted to 50% transparence to show the residue details on the binding interface.
  2. Four contact regions within the YAP‐WW1/SMAD7‐PY complex were shown in details from the representative top cluster structures. Residues from SMAD7‐PY motif peptide were labeled in purple. Hydrogen bond is indicated in blue line.
  3. The binding type and the corresponding frequency rate were shown for the indicated inter‐ and intramolecular residue pairs.
  4. Simulation analysis of apo YAP‐WW1 domain and its indicated mutants. RMSD value for each mutant simulation (referenced against the average apo YAP‐WW1 domain) was shown.
  5. Average structures of the indicated YAP‐WW1 mutant/SMAD7‐PY complexes.
  6. The average distance between SMAD7‐PY motif peptide and the indicated WW domains was summarized in a table.