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TitleThe Cryo-EM structure of human CD163 bound to haptoglobin-hemoglobin reveals molecular mechanisms of hemoglobin scavenging.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10871, Year 2024
Publish dateDec 30, 2024
AuthorsAnders Etzerodt / Jakob Hauge Mikkelsen / Morten Torvund-Jensen / Dorle Hennig / Thomas Boesen / Jonas Heilskov Graversen / Søren Kragh Moestrup / Justin M Kollman / Christian Brix Folsted Andersen /
PubMed AbstractCD163, a macrophage-specific receptor, plays a critical role in scavenging hemoglobin released during hemolysis, protecting against oxidative effects of heme iron. In the bloodstream, hemoglobin is ...CD163, a macrophage-specific receptor, plays a critical role in scavenging hemoglobin released during hemolysis, protecting against oxidative effects of heme iron. In the bloodstream, hemoglobin is bound by haptoglobin, leading to its immediate endocytosis by CD163. While haptoglobin's structure and function are well understood, CD163's structure and its interaction with the haptoglobin-hemoglobin complex have remained elusive. Here, we present the cryo-electron microscopy structure of the entire extracellular domain of human CD163 in complex with haptoglobin-hemoglobin. The structure reveals that CD163 assembles into trimers (and to some extent dimers), binding haptoglobin-hemoglobin in their center. Key acidic residues in CD163 interact with lysine residues from both haptoglobin and hemoglobin. Calcium-binding sites located near the haptoglobin-hemoglobin interface in CD163 provide explanation for the calcium dependence of the interaction. Furthermore, we show that the interaction facilitating CD163 oligomerization mimics ligand binding and is also calcium dependent. This structural insight into CD163 advances our understanding of its role in hemoglobin scavenging as well as its broader relevance to structurally related scavenger receptors.
External linksNat Commun / PubMed:39738064 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.52 - 5.2 Å
Structure data

50444

9fhb

EMDB-50444, PDB-9fhb:
Cryo-EM structure of human CD163 SRCR2-4 in complex with haptoglobin-hemoglobin
Method: EM (single particle) / Resolution: 3.87 Å

50570

9fmu

EMDB-50570, PDB-9fmu:
Cryo-EM structure of human CD163 SRCR1-9 in complex with haptoglobin-hemoglobin
Method: EM (single particle) / Resolution: 4.46 Å

50600

9fno

EMDB-50600, PDB-9fno:
Cryo-EM structure of human CD163 SRCR1-9 in complex with haptoglobin-hemoglobin
Method: EM (single particle) / Resolution: 5.2 Å

PDB-9fnm:
Structure of human haptoglobin
Method: X-RAY DIFFRACTION / Resolution: 2.52 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsENDOCYTOSIS / Scavenging receptor / oxygen transport / complex / hemolysis / inflammation / PROTEIN BINDING / acute phase / hemoglobin binding / reactive oxygen specis

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