Figure 1 | Scientific Reports

Figure 1

From: Structural prerequisites for CRM1-dependent nuclear export signaling peptides: accessibility, adapting conformation, and the stability at the binding site

Figure 1

NES consensus patterns used in this study. For the hydrophobic positions, Φ1–4 are Leu, Ile, Val, Met, or Phe, and for the Φ1 and Φ2 positions, Thr or Ala is allowed for one position. Φ0 is not restricted to the hydrophobic amino acids. In the reverse classes, the criteria are applied in the opposite direction, and one of the Φ0 or Φ1 should be Leu, Phe, or Met. The spacer residues (x) can be any amino acid, but several positions have exceptions. The spacers in Φ2 [X]nΦ3XΦ4 (or Φ0XΦ1[X]nΦ2 in reverse classes) do not allow to have Pro or Trp. For class 4, at least one residue of the spacers in Φ3XXXΦ4 should be Pro to make a turn (as observed in the X-ray crystal structure of CRM1-X11L2 peptide).

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