Fig. 1: The structure of CD163 bound to HpHb.
From: Scavenger receptor CD163 multimerises to allow uptake of diverse ligands
a The structure of a trimer of the CD163 ectodomain bound to the HpHb complex. The three copies of CD163 are shown in three shades of blue. HpSP domain is green, the α-subunit of Hb is red and the β-subunit of Hb is orange. b The structure of a dimer of the CD163 ectodomain bound to the HpHb complex, coloured as in (a). c An alignment of the three CD163 molecules found in the trimeric complex, aligned on SRCR5, with the SRCR domains labelled. d A close-up of the interfaces between two pairs of CD163 subunits with the red dotted line showing the different distances between the Cα atoms of residues 561 and 804 in these two interfaces. e An alignment of each pair of CD163 ectodomains observed in the trimeric and dimeric complex, with each aligned on SRCR7 of the left-hand CD163. The right-hand CD163 molecules from the trimer are coloured as in (a). and in pink for the CD163A from the dimer. Dashed lines indicate the maximum degree of tilting of the arm of CD163 in these structures.
