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. 2019 Aug 22;10:2007. doi: 10.3389/fimmu.2019.02007

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Copyright © 2019 Pedersen, Gadeberg, Thomas, Wang, Joram, Jensen, Mazarakis, Revel, El Sissy, Petersen, Lindorff-Larsen, Thiel, Laursen, Fremeaux-Bacchi and Andersen.

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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Structure of the FP oligomerization interface and analysis of its stability. (A) Outline of the interface between TB and TSR4 of FP. Important residues are shown in an all-atom stick representation. The O-linked glycan on T272 is directly involved in the interaction of TSR4 with the TB domain through a hydrogen bond (dotted line). (B) As panel A but presenting the interface between TSR1 and TSR6. (C) Western blot analysis of cell supernatants obtained with different FPht mutants. To account for differences in total amount of cells a western blot of GAPDH from the cell pellet was performed using the same amount of sample volume.