ArticleNature communications2024
The Cryo-EM structure of human CD163 bound to haptoglobin-hemoglobin reveals molecular mechanisms of hemoglobin scavenging.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Engineered haptoglobin β fusion protein targets myoglobin and ameliorates rhabdomyolysis-associated acute kidney injury.EMBO molecular medicine · 2026Article
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Review
- Precision medicine approach to coronary artery disease: Haptoglobin phenotype‑guided risk assessment.Molecular medicine reports · 2026Article
- Structural basis for hemoglobin scavenging by CD163 reveals mechanism of ligand promiscuity.PLoS biology · 2026Article
- Molecular and spatial specialization of lung interstitial macrophage subsets: beyond chemokines.Frontiers in immunology · 2026Article
- A Hemoglobin-Based Nanoparticle Delivery System Enhances the Pharmacokinetics and Efficacy of Tigecycline inBME frontiers · 2026Article
- Strength in numbers: how multimerization drives HpHb uptake by CD163 scavenging receptor.Nature communications · 2025Article
- Calcium-dependent oligomerization of scavenger receptor CD163 facilitates the endocytosis of ligands.Nature communications · 2025Article
- Scavenger receptor CD163 multimerises to allow uptake of diverse ligands.Nature communications · 2025Article
- Structural elucidation of the haptoglobin-hemoglobin clearance mechanism by macrophage scavenger receptor CD163.PLoS biology · 2025Article
- Identification and validation of core biomarkers for sepsis: a comprehensive analysis using bioinformatics and machine learning.Frontiers in immunology · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
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.
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