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. 2023 Oct 28;14:6894. doi: 10.1038/s41467-023-42229-y

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Domain diagram of human cortactin (UniProt: Q60598), highlighting the sequence of the fragment Cort_1-76 used in the cryo-EM structure and residues D20-V29 implicated in Arp2/3 complex binding. b Cryo-EM map of Cort_1-76 (orange) bound to Arp2/3 complex. Arp2/3 complex subunits are colored as follows: Arp2, cyan; Arp3, green; ArpC1, yellow; ArpC2, ArpC3, and ArpC5, light gray; ArpC4, dark gray. The inset shows cortactin residues D20-V29 and the corresponding cryo-EM map in orange, and the binding site on Arp3 (green cartoon representation with gray side chains). See also Supplementary Fig. 2a. c Superimposition of the A domains of cortactin (orange), N-WASP (magenta, PDB code 6UHC), and Arpin (blue, PDB code 7JPN) on Arp3 (green and gray). Insets show the binding site (gray) of the A domains and the binding pocket of the conserved tryptophan of the three proteins. The sequences of the three A domains are shown on the side, vertically aligned according to the structures. Note that cortactin binds the site on Arp3 with inverted polarity compared to N-WASP and Arpin.