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. 2018 Oct 5;11(1):58–74. doi: 10.1080/19420862.2018.1522178

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© 2018 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — Allosteric Fab-FcγRI communication is via limited residue contact pathways, highlighting the importance of conformational population shift in allosteric signal transduction. a. Motion correlation among residues of different clusters. Residues with highly (anti)correlated motion are red (blue). The cluster numbers correspond to the clusters in Figure 2. b. Optimal and suboptimal paths connecting plausible allosteric sites from Aβ to FcγRI D3 domain in the Fab-FcγRI- Aβ complex (cluster10). Optimal and suboptimal paths are colored by red and yellow, respectively.