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. 2021 Mar 25;12(17):5977–5993. doi: 10.1039/d1sc00165e

Fig. 2. Comparison of unconstrained/constrained Aurora-A bound TPX2 peptides; (a) view of Aurora-A (blue) bound to stapled TPX2 (red, hydrocarbon staple: orange, PDB: 5LXM) with native TPX2 (purple, PDB: 1OL5) overlaid. TPX2 residues known to be crucial for binding to Aurora-A are shown as sticks to highlight the conserved binding mode between stapled and native TPX2; (b) Tyr8, Tyr10, Asp11, Trp34 and Phe35; (c) Phe16 and Phe19; (d) orientations of residues Lys38 and Glu36 differ, promoting additional electrostatic interactions (dashed lines) between peptide and Aurora-A.45.

Fig. 2