Amino acid alignment of transcribed Chinese egret MHC class II β chain sequences compared with those of other bird species.

<p><i>Dots</i> indicate identity with the Egeu-DAB1*01 sequence, <i>dashes</i> indicate gaps. Conserved residues characteristic of classical class II β chain molecules [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0074185#B41" target="_blank">41</a>] are <i>shaded</i>. Amino acids that contact the peptide-binding region in the human DRβ molecule [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0074185#B42" target="_blank">42</a>] are indicated with a <i>plus sign</i> (on alignment top). Cysteine bridges in the β1 and β2 domains are indicated by <i>brackets</i>. Residues in the β2 domain that are implicated in CD4 binding in humans are boxed. Species and accession numbers for other bird sequences are as follows: ArciDAB1 Grey Heron, HM991016; ArciDAB2 Grey Heron, HM991017; TyalDAB1 Barn Owl, EU442606; TyalDAB2 Barn Owl, EU442607; ApowDAB01 kiwi, HQ639683, ApowDAB05 kiwi, HQ639685; GagaBLBII chicken, NM_001044679.