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. 2016 Apr 8;26(5):543–555. doi: 10.1038/cr.2016.45

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Copyright © 2016 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 Unported License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/

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The last residue of TDIF is recognized by a set of highly conserved amino acids of PXY. (A) Detailed interactions of the conserved TDIF^Asn12 with PXY^LRR. The side chains of some amino acids from TDIF and PXY^LRR are shown in purple and yellow orange, respectively. Red dashed lines indicate hydrogen bonds or salt bridges. (B) Sequence alignment of PXY^LRR with other CLE receptors around the TDIF^Asn12-interacting region. (C) The two consecutive LRRs recognizing the last residue of TDIF are stabilized by a conserved disulfide bond. The sulfur atoms are colored in cyan. (D) Sequence alignment of PXY^LRR with other known CLE receptors around the disulfide bond region. For (B and D), conserved and similar residues are boxed with red ground and red font, respectively. Conserved motifs are boxed with blue frames.