Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-IMG-124883

Xenbase Image ID: 124883


Figure 10. Threaded models of Shaker-IR and I287D+F324D based on Kv1.2/Kv2.1 chimera structure. (A) I287 and F324 are closely apposed in threaded Shaker-IR model. Side (left) and top (right) views are shown. S1 (light blue), S2 (yellow), S3 (red), and S4 (dark blue) transmembrane segments are pictured in cartoon form. Selected side chains are shown: I287 in S2 and F324 in S3b (green); acidic residues E283 and E293 in S2 and D316 in S3 (yellow and red); basic residues R362, R365, R368, R371, K374, and R377 in S4 (gray and blue). A subset of side chains are labeled to provide landmarks. S4 positively charged residues are labeled with a generic nomenclature (R1–R6). Dotted black line connects atoms of I287 and F324 that are ∼4.0 Å apart. (B) Aspartate residues introduced at I287D and F324D are closely apposed and located at the interface between the voltage sensor domain and the hydrophobic core of the membrane. Side (left) and top (right) views of I287D+F324D double-mutant model. Color code and labeling are the same as in A, except that the mutations I287D and F324D are shown in green and red. Dotted black line connects oxygen atoms of D287 and D324 that are ∼3.8 Å apart. (C) I287D and F324D are able to simultaneously coordinate a Mg2+ ion. Side (left) and top (right) views of I287D+F324D double-mutant model. Transmembrane segments S1–S4 are shown in ribbon form using the same color code as in A. Bound Mg2+ ion is shown as a green sphere. Color code and labeling are the same as in B. The figure was made using PyMOL (DeLano, 2002).

Image published in: Lin MC et al. (2010)

© 2010 Lin et al. Creative Commons Attribution-NonCommercial-ShareAlike license

Larger Image
Printer Friendly View

Return to previous page