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. Author manuscript; available in PMC: 2016 Jan 6.
Published in final edited form as: Structure. 2014 Dec 18;23(1):173–182. doi: 10.1016/j.str.2014.11.006

Fig. 5.

Fig. 5

Interface between actin protomers in T1- and T2- actins. 3D-reconstructions are front (A and C) and side (B, D and E) views. (A) Longitudinal contacts in T1-actin reside in the 39–47 region located in SD2 of the lower protomer (red) and region 285–291 (blue) in SD3 of the upper protomer. (B) Lateral interactions are likely to involve residues 112–118 (orange) and 368–371 (green) in SD1 of the upper protomer, and 195–205 (magenta) in SD4 along with the hydrophobic plug (264–272 in cyan) in the lower protomer. (C) Longitudinal contacts in T2-actin are similar to the T1-actin, but also may include residue 60–64 (marked in red). (D) lateral interactions in T2-actin map to the same regions as in T1-actin except for the112–118 region. (E) Residues linked to human diseases are shown as spheres in different colors. Note that these residues are at the interfaces between protomers in the tilted actin.