Fig. 3: Interactions of Arpin and N-WASP with Arp2/3 complex.
From: Molecular mechanism of Arp2/3 complex inhibition by Arpin
a, b Superimposition of Arpin_CA-Arp3 (marine blue and green) onto N-WASP-Arp2 (a) and N-WASP-Arp3 (b) (magenta and gray). c The contact surface (orange) of Arpin on Arp3 involves Arpin’s C-helix and the A domain, whereas the negatively charged linker between these two regions is flexible and does not participate in specific contacts. d–g Comparison of the specific interactions of the A domain (d and f) and C-helix (e and g) of Arpin and N-WASP with Arp3 (green with orange side chains). Insets show details of the interactions of the C-helices of Arpin (e) and N-WASP (g) with the C-terminal tail of Arp3. The inset in part e shows a comparison of the C-terminal tail of Arp3 in both structures (green-orange, Arpin structure; gray, N-WASP structure.
