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. 2021 Oct 7;9:719949. doi: 10.3389/fchem.2021.719949

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Copyright © 2021 Lin, Lin, Wu, Liu, Cheng, Xu, Li and Dong.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) The structure of the Fascin-inhibitor complex. Junctions between β-trefoils 1 and 2, β-trefoils 1 and 4 contain two actin-binding sites respectively, and another actin-binding site locates on β-trefoils 3 (Figure 1A). (B) Inhibitor NP-G02-029 and the binding pocket. (C) Protein−NP-G2-029 interactions are represented by an asteroid plot. The inner ring represents direct interactions. The outer ring represents indirect interactions. The size of the ball is the interaction-number proportion in atomic scale. The colors of residues correspond to their secondary structures. (D) Secondary structure connection of Fascin. The bottom panel shows the secondary structure (β-sheets and α helixes) with their respective colors. Arrows stand for β-sheets, rectangles stand for α helix. N-ter, N terminus; C-ter, C terminus. PDB ID: 6B0T. Structure visualized by PyMOL (Rigsby and Parker, 2016).