Skip to main content
. 2020 Jun 19;117(27):15554–15564. doi: 10.1073/pnas.2002483117

Fig. 5.

Fig. 5.

Assessing the effect of Hp glycosylation and proteolytic processing on Hp–Hb binding based on the structure of the human Hp–Hb–CD163 complex (PDB ID code 4WJG). (A) Structure of Hp 1-1 (gray) fully saturated with two Hb (αβ) dimers (green). (B) Structure of one Hp (αβ) unit bound to Hb (αβ) highlighting the Asn residues of Hp-β that carry biantennary N-glycans displayed in orange balls and sticks, respectively, revealing their proximity to the interaction site. (C) Cleaved Hp-α1R chain fitted into the available structural model of Hp 1-1 (shown as a pink cartoon) reveals that the C-terminal Arg102 is in the proximity of the Hb-α molecule (green).