Brownian Dynamics Simulation of Nucleocytoplasmic Transport: A Coarse-Grained Model for the Functional State of the Nuclear Pore Complex
Figure 7
The cargo-complex interacting with FG-repeat domains via hydrophobic patches on the convex surface of the kap-β[46], [73].
Kap-β has a boat-like shape [8] and the localization of the binding spots on its surface has led to the idea of a “coherent FG-binding stripe” instead of discrete binding spots [46]. In our model, we take into account this fact by considering a ‘hydrophobic arc with limited capacity’ on the cargo surface. This arc possesses eight hydrophobic binding spots, and thus, is able to simultaneously interact with up to eighth FG-motifs. The magnification on the right shows a closer depiction of the cargo-complex with the crystal structure of the kap-β (blue) interacting with FG-repeats (red) on its convex surface (1F59, pdb bank). Also, the average path of a 15 nm cargo-complex during translocation is shown in purple. The path is averaged over 150 independent simulations. As it can be seen, the cargo-complex is primarily attached to the FG-layer during its translocation.