Fig. 3: Comparison of unliganded B44:05-T73C-6mer (7TUD) with the complex of Tapasin–B44:05 (7TUE) reveals displacement of α2-1 helix and β-sheet floor of peptide binding groove of B44:05.
From: Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation
The indicated models were superposed based on residues 54-84 of the MHC-I α chain. a–d Views of the tapasin–B44:05 interface are shown, with 1σ 2mFo-DFc map for c, d. Letters in panel a denote the regions enlarged in c, d and e. Movement of α2-1 helix (a, b, f, g), and c, local contacts of Glu11 and Lys20, and d, portion (Glu72-Phe76) of the long strand–loop Glu72-Lys84, and e, of the hairpin loop Gln189-His195 are shown. Yellow dotted lines indicate H-bonds with distances noted in Å.
