Fig. 4: The F2-R12 interaction does not substantially contribute to the closed conformation of talin. | Nature Communications

Fig. 4: The F2-R12 interaction does not substantially contribute to the closed conformation of talin.

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

Fig. 4

a In the previously reported 6.2 Å resolution structure (PDB entry 6r9t)11, the F2-R12 interdomain interactions occur between Lys-272 with Glu-2288 and Lys-274 with Gln-2285. b, c, Our (b) talin3.4 structure and (c) talin2.7 structure display similar interactions as previously reported (see panel a). d In our talin5.5 structure, Lys-274 interacts with Glu-2288 instead of Gln-2285. e Superposition of the F3 and R9 domains that keep talin in its closed conformation shows flexibility in their corresponding F2 and R12 domains. The spheres represent the Cα positions of residues 272 and 2289, respectively.

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