Fig. 6: Analysis of polymorphic insertions in bat MHC-I based on AF2 structure prediction.
From: Amino acid insertion in Bat MHC-I enhances complex stability and augments peptide presentation

a Structural prediction of Mylu-B*67:01, Mylu-B*67:01ΔMQQPW, and their complexes with P1 peptide by AF2 and AF2-Multimer. b Precise prediction of the structures of pMylu-B*67:01-P1 and pMylu-B*67:01ΔMQQPW-P1 by AF2-Multimer. The predicted structures showed good consistency with the resolved crystal structures, especially regarding the conformation of both the MQQPW insertion and the P1 peptide. c Comparison of amino acid sequences near insertion and AF2 prediction of existing bat MHC-I structures. Sequences with five, three, and zero amino acid insertions were represented by orange, blue, and cyan parts, respectively. The pairs of positively and negatively charged residues that appear after insertion were marked in pink. The sequence logos showed the polymorphism of the insertion sequences.