Fig. 7: myr-Arf1 interaction with its effectors and the basis of conformational selection. | Nature Communications

Fig. 7: myr-Arf1 interaction with its effectors and the basis of conformational selection.

From: Myr-Arf1 conformational flexibility at the membrane surface sheds light on the interactions with ArfGAP ASAP1

Fig. 7

2D 1H-15N spectra of myr-Arf1⦁GTP in the presence of 100 µM ASAP1 PH (myr-Arf1-GTP:ASAP1 PH = 1:1), shown as A 1H-15N TROSY-HSQC and B 1H-15N HSQC spectra. Asparagine and glutamine side-chain amine groups are circled. C Arf1 G domain presents multiple states (center ensemble) to recognize signaling partners. NMR and MD analyses identify three populated conformations (S1 (blue), S2 (orange), S3 (green) with switch 1-switch 2 highlighted in yellow) that mutually exchange on the surface of the membrane. Postulated recognition of the S3 conformation by ASAP1 PZA is modeled based on the structure of the Arf6:ASAP3 GAP complex48 (ASAP3 shown as tan ribbon and surface based on PDB: 3LVQ; S3 state of myr-Arf1 in the membrane shown as green ribbons with switch 1, switch 2 in yellow ribbon and the myr-chain in red). A putative position of the ASAP1 PH domain (tan colored ellipsoid, positioned N-terminal to the GAP and ankyrin domains), which interacts with the membrane surface16, suggests how binding to PH at the membrane would form a motionally restricted complex (panels A and B). Images created using Chimera75.

Back to article page