Figure 1

Schematic representation of the structure and domain organization of membrane-bound CD163. CD163 consists of a 1003 amino acid extracellular portion with 9 class B scavenger receptor cysteine-rich (SRCR) domains, with domains 6 and 7 separated by a 31 amino acid linker. This linker is composed of many proline, serine and threonine residues (PST). Another PST linker connects the last SRCR domain to the transmembrane segment, which is made up of 24 amino acids. The intracellular cytoplasmic domain ranges from 49 to 89 amino acids that contain consensus sequences for phosphorylation and internalization.