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. 2017 Oct 5;8(10):259. doi: 10.3390/genes8100259

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© 2017 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Structural modeling results of the Tumour Necrosis Factor (TNF) homology domain of p.Val351Phe-mutated (A, C) and wild-type (B) Ectodysplasin A (EDA) proteins. (A) The p.Val351Phe mutation was located on the monomer–monomer interaction surface of the three monomers. (B) In the wild-type EDA protein, there was a small gap between p.Val351 and p.Val250 of the adjacent monomer. (C) In the p.Val351Phe-mutated EDA protein, the mutated p.351Phe was too large and extruded with p.Val250 of the adjacent monomer.