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. 2022 Nov 18;13:1041315. doi: 10.3389/fimmu.2022.1041315

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Copyright © 2022 Sultan, Adawi, Kol, McCourt, Adawi, Baram, Tal, Werner, Lev, Snapper, Barel, Konnikova, Somech and Shouval

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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Identification of RIPK1 mutations in index patients. Figure depicts chromatogram of RIPK1 gene sequencing at the site of designated mutations for (A) Patient 1 and (B) Patient 2. Visualization of the structural consequences demonstrates that (C) Ala194 is buried in RIPK1 kinase domain C’ lobe (PDB: 4ITJ), and that (D) the mutation of Ala194 to Thr introduces clashes (indicated by red disks) with Tyr212 and His197. (E) Thr645 is found on the surface of the death domain of RIPK1 and mediates a hydrogen bond to a nearby water molecule (PDB: 6AC5). (F) The mutation of Thr645 to Methionine displaces this water molecule and may affect local structure and death domain dimerization.