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. 2021 Mar 26;16(3):e0247335. doi: 10.1371/journal.pone.0247335

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© 2021 Mason et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 6 — (A) Head-to-tail interactions in EphB6-ECD. Similar to the previously published A-class ectodomain structures, the LBD (cyan) and FN (green) domains of neighboring EphB6 molecules form an interface in the unliganded receptors. (B) The zoom-in shows the interacting amino acid residues. (C) Comparison of the head-to-tail interactions in EphB6-, A4- and A2-ECDs. (Left) EphB6-LBD (cyan) bound to EphB6-FN of a neighboring molecule (yellow) in the crystals of the unliganded EphB6-ECD; (Center) EphA4-LBD (blue) bound to the EphA4-FN of a neighboring molecule (orange) in the crystals of unliganded EphA4-ECD; (Right) EphA2-LBD (green) bound to the EphA2-FN of a neighboring molecule (red) in the crystals of unliganded EphA2-ECD.