Fig. 2: Close-up view of the talin R3 domain. | Nature Communications

Fig. 2: Close-up view of the talin R3 domain.

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

Fig. 2

a Superposition of the four α-helices of R3 from our talin2.7, talin3.4, talin3.7, and talin5.5 structures. The R3 four-helix bundle is highlighted and color-coded in orange, yellow, green, and blue, representing α-helices 1 through 4, respectively. VBS, vinculin binding site. b The NMR structure of the isolated R3 domain (PDB entry 2l7a)22 shows the amino terminus (magenta) extending its first α-helix. c In the context of the full-length polypeptide chain, the R3 amino terminus (magenta) is bent to position R3 roughly perpendicular to R2. d Coulomb potential map displaying the connection between R2 and R3 (magenta). e Close-up view of the interactions of R3 (Asn-881, Asp-882, and Gln-887) with R10 (Glu-1959, His-1963, Gln-1969, and Arg-1973) and R11 (Gln-2049). R3 appears responsible for maintaining R11 in its firm state, contrasting with the R12 conformation changes, a notion that is well supported by the local resolution maps.

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