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. 2021 Sep 28;22(11):e52675. doi: 10.15252/embr.202152675

Figure 6. Anchor of PPM1H is a folding motif.

Figure 6

  1. Interactions between the anchors of PPM1H against the electrostatic surface of the core catalytic domain. The region is placed in context with the dotted box on a ribbon model of PPM1H (right).
  2. Incremental deletions of the N‐terminal 37 to 44 residues, one residue at a time. Upon deletion of R43 (44‐end), a reduced level of soluble PPM1H expression has no significant catalytic activity.
  3. Sequence alignment of the N‐terminal regions of the evolutionarily related PPM1H/J/M enzymes. The degree of conservation is above the alignment, and residue numbers correspond to PPM1H. A conserved anchor motif (RPxFL) is annotated below the sequences.