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. 2017 Oct 24;8:1111. doi: 10.1038/s41467-017-01263-3

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Structure of mature rhGAA. a Proteolytic treatment of rhGAA. b Schematic representation of the sequence of GAA. Myozyme^® rhGAA used in ERT starts at residue Q57. Domains corresponding to the rhGAA structure are colored as in c, with the regions removed by treatment with α-chymotrypsin colored in white. c Cartoon representation of the structure of rhGAA consisting of the trefoil type-P domain (salmon), the N-terminal β-sheet domain (slate), the catalytic GH31 (β/α)₈ barrel domain (green) with insert I (gold) and insert II (pink), and the proximal (orange) and distal (teal) β-sheet domains. Catalytic residues (magenta) and glycan chains (grey) are depicted as sticks. Dashed lined circles highlight peptide portions removed by proteolysis with α-chymotrypsin before crystallization. (SP, signal peptide; PP, propeptide)