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. 2020 May 29;8:405. doi: 10.3389/fcell.2020.00405

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Copyright © 2020 Soll, Eisen, Vargas, Medeiros, Hammar and Morgan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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α-Syn-112 splice isoform. (A) Domain diagram of α-syn-140 and α-syn-112 showing the result of exon 5 deletion. (B) (top) The NMR structure of human α-syn-140 bound to lipid micelles (Ulmer et al., 2005), and (bottom) predicted structure of α-syn-112 (UCSF Chimera software). α-Syn-112 is predicted to have a slightly extended alpha helix. (C) Coomassie-stained SDS-PAGE gel and Western blot showing the size difference between α-syn-140 (14 kDa) and α-syn-112 (12 kDa). In the Western blot, the higher molecular weight bands represent minor fractions of dimeric α-syn-140 and α-syn-112.