File:An-electrostatic-mechanism-for-Ca2+-mediated-regulation-of-gap-junction-channels-ncomms9770-s2.ogv
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[edit]DescriptionAn-electrostatic-mechanism-for-Ca2+-mediated-regulation-of-gap-junction-channels-ncomms9770-s2.ogv |
English: Supplementary Movie 1 Ca2+ coordination sites reside at the interface between adjacent subunits, near the entrance to the extracellular gap, where local conformational rearrangements enable Ca2+-chelation. Each of the 12 Ca2+ binding sites is comprised of the G45-O and the E47 carboxylate from one subunit, and the E42 carboxylate of the adjacent subunit. The Ca2+-bound and Ca2+-free structures were superimposed, and the morph conformations tool in Chimera was used to create a conformational trajectory between the two structures (morph model, cyan; Ca2+ atom, yellow; coordinating atoms, sticks). |
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Source | Video file from Bennett B, Purdy M, Baker K, Acharya C, McIntire W, Stevens R, Zhang Q, Harris A, Abagyan R, Yeager M (2016). "An electrostatic mechanism for Ca2+-mediated regulation of gap junction channels". Nature Communications. DOI:10.1038/ncomms9770. PMID 26753910. PMC: 4730032. | ||
Author | Bennett B, Purdy M, Baker K, Acharya C, McIntire W, Stevens R, Zhang Q, Harris A, Abagyan R, Yeager M | ||
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This file is licensed under the Creative Commons Attribution 4.0 International license.
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 16:51, 29 October 2016 | 2.8 s, 640 × 480 (111 KB) | Open Access Media Importer Bot (talk | contribs) | Automatically uploaded media file from Open Access source. Please report problems or suggestions here. |
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Short title | Supplementary Movie 1 |
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Author | Bennett B, Purdy M, Baker K, Acharya C, McIntire W, Stevens R, Zhang Q, Harris A, Abagyan R, Yeager M |
Usage terms | http://creativecommons.org/licenses/by/4.0/ |
Image title | Ca2+ coordination sites reside at the interface between adjacent subunits, near the entrance to the extracellular gap, where local conformational rearrangements enable Ca2+-chelation. Each of the 12 Ca2+ binding sites is comprised of the G45-O and the E47 carboxylate from one subunit, and the E42 carboxylate of the adjacent subunit. The Ca2+-bound and Ca2+-free structures were superimposed, and the morph conformations tool in Chimera was used to create a conformational trajectory between the two structures (morph model, cyan; Ca2+ atom, yellow; coordinating atoms, sticks). |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2016-01-12 |