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. 2010 May 19;98(10):2179–2188. doi: 10.1016/j.bpj.2010.01.049

Figure 2.

Figure 2

The main hinges as inferred from the eight slowest modes, presented on the 3D model structure of Kv1.2 (5). Only two chains are shown: chain A (left) in colors and chain C (right) in gray. The flexible segment identified in the three slowest modes, containing the S3 and S4 helices and the linker in chain A, is in dark blue. The main chain atoms of the amino acids that were found to serve as hinges are presented as spheres. The hinge in the selectivity filter (T373-D379) is in yellow. The hinge in the S6 helix (I402-V410) is in magenta. The hinge between the linker and the S5 helix (M325-L328) is in green. The hinges in the S1 helix (C181), S2 helix (S217), and S3 helix (V261) are in cyan. These hinges were identified in the first three modes. The hinge in the S4 helix (F302, orange) was identified in the next five modes (4–8). The network of hinges and rigid elements appears to couple between the VSD and PD. The figure was prepared using PyMol (71).