Fig. 4: Model of ASAP1 PH:myrArf1 complex at the membrane surface. | Nature Communications

Fig. 4: Model of ASAP1 PH:myrArf1 complex at the membrane surface.

From: An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function

Fig. 4

A Snapshot representative of the model of the complex between myrArf1 (blue ribbon) with the GTP nucleotide represented as ball and stick and ASAP1 PH (gold ribbon) at the membrane surface. B ASAP1 PH: Arf interaction counts plotted against residue number and plotted on the model. Data were averaged over all MD trajectories with a cutoff of 3.5 Å to detect nonhydrogen proximities. C Key interactions at the interface. Stable intermolecular salt bridges and residues forming the hydrophobic cluster comprising Phe51, Trp66, Ile74, Leu77 and Trp78 on Arf1 and Leu 386 (β45 loop), His405 (β67 loop) and Leu 434, Ala 437 and Phe438 (end of the C-terminal helix) on ASAP1 PH are shown. All images created using Chimera56. Source data are provided as a Source data file.

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