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. 2023 Apr 14;14:1156219. doi: 10.3389/fimmu.2023.1156219

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Copyright © 2023 Jia, Feng, Dooley, Zou and Wang

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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ScCD8αα possess a canonical binding cavity. The composition of the binding cavities in representative vertebrate CD8αα structures are shown. Molecular surfaces are rendered in white, with residues key to dimeric interaction highlighted blue. (A) The cavity of ScCD8αα, the side chains of cavity residues are shown as sticks and colored magenta. (B) The cavity of grass carp CD8αα, the side chains of cavity residues are shown as sticks and colored lime green. (C) The cavity of chicken CD8αα, the side chains of cavity residues are shown as sticks and colored yellow. (D) The cavity of human CD8αα, the side chains of cavity residues are shown as sticks and colored pink. (E, F) Comparison of key amino acids in the cavity of CD8αα structure in selected species, the residues and the distance between His28 and Phe33 are labeled.