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. 2021 Mar 2;9:622390. doi: 10.3389/fcell.2021.622390

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Copyright © 2021 Lückstädt, Bub, Koudelka, Pavlenko, Peters, Somasundaram, Becker-Pauly, Lucius, Zunke and Arnold.

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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Molecular model of TEP1 fits best into 3D reconstruction of CD109. Thioester-containing protein 1 (TEP1r, PDB ID: 2PN5) matches best with the negative stain transmission electron microscopy (TEM)-generated 3D model. 2PN5 homology model is outlined within the 3D model (A) or by itself (B) rotated in 90° angles with colored functional regions; legend shown in panel (D). For quality reasons, map values were calculated and displayed in tabular view in panel (C). C-terminus expressed in yellow gives an idea of the structural orientation of CD109 on the cell surface (D) Connected to the GPI anchor. The bait region is shown in red with possible cleavage sites given for meprin β and BMP-1; the thioester region is in orange, and its structural proximity to the reactive thioester-defining hexapeptide motif is in green; the furin cleavage site oriented toward the cell membrane is in blue.