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. 2013 Feb;141(2):151–160. doi: 10.1085/jgp.201210888

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© 2013 Hoshi and Armstrong

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 3. — An expanded view of the outer mouth of the selectivity filter of the K_v1.2-2.1 chimera and two simulated mutations. The four outermost Y373 carbonyl oxygens outline the pore, but only one tyrosine is shown in full. (A) The conducting conformation of the filter mouth, taken from the K_v1.2-2.1 chimera. Y373 (Y445) has close contacts with W362 (W434) and V377 (T449). (B) A simulated mutation of the K_v1.2-2.1 chimera that replaces V377 (T449) with V377A (T449A), allowing Y373 (Y445) to rotate and dilate the filter mouth. The mutation in effect deletes the two γ carbons of V377 (T449), removing a contact that locks Y373 (Y445) in the conducting, nondilated position. (C) Simulated mutation W362 (W434) of the K_v1.2-2.1 chimera that replaces W362 (W434) with F362 (F434). Relative to W362 (W434), F362 (F434) is rotated clockwise in this view; it presses against the ring of Y373 (Y445), causing Y373 (Y445) to rotate counterclockwise, dilating the filter mouth. The angle of view is the same throughout the figure. The images were prepared using MacPyMol (version 0.99).