Figure 1. A prevalent target-binding cleft in actin.

Figure 1

A prevalent target-binding cleft in actin. A) Ribbon representation illustrating the “conventional” view of actin. Two diametrically opposed clefts, the nucleotide cleft and the target-binding cleft, effectively separate the actin molecule into two large domains. The polypeptide chain goes across domains only twice. The α-helix between amino acids Ile 136 and Gly 146, shown in green, serves as a hinge for inter-domain motions. This α-helix lines the target-binding cleft. B) Surface representation of actin (same orientation as in part A), showing the target-binding cleft in green. C) Two molecules of actin along one filament strand of Holmes' F-actin model.43

From: A Common Binding Site for Actin-Binding Proteins on the Actin Surface

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