Fig. 3: The head-tail interaction, F3-R9, keeps talin in its closed conformer. | Nature Communications

Fig. 3: The head-tail interaction, F3-R9, keeps talin in its closed conformer.

From: High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling

Fig. 3

a The superposition of the F3 domains of the F2-F3 in complex with R9 crystal structure (PDB entry 4f7g)49 onto our talin2.7 structure reveals the relative domain movement of R9. The individual α-helices of the R9 five-helix bundle are color-coded spectrally, labeled for the crystal structure (PDB entry 4f7g), and underlined for talin2.7. b In the crystal structure (PDB entry 4f7g), temperature factors are below 90 Å2 for F3 and higher (up to ~120 Å2) for R9. c, d Superposition of F3 in our talin2.7 structure (c) and the crystal structure (d) aligns Ser-362 and Ala-360 of F3 but shows a significant relative shift in Leu-1680, Val-1683, and His-1755 of R9.

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