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. 2017 Feb 1;45(6):3378–3394. doi: 10.1093/nar/gkx066

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — Models of A3C dimerization. (A) For hA3C, N115 (chain A) is 4.7 Å away from the backbone of R44 (chain B). (B) In contrast, a model of cA3C K115 (chain A) positions the backbone of R44 (chain B) only 3.0 Å away. This distance could indicate a new hydrogen bond with potential to stabilize the dimer between chains A and B. (C) In hA3C, S188, shown with van der Waal space filling dots, packs closely to F126 and N132, but does not clash with either. (D) In contrast, a model of hA3C shows how I188 would clash with F126 and N132 (arrows indicating overlap of van der Waal space filling dots). Conformational changes, potentially including a repositioning of the helix to enable formation of an A–B dimer, would be needed to accommodate this amino acid variant.