8A59

C-type lectin-like domain (CTLD) and Sushi-like domain of human CD93

Summary for 8A59

• Entry DOI: 10.2210/pdb8a59/pdb
• Descriptor: Complement component C1q receptor, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: c-type lectin-like domain, ctld, sushi-like domain, dimerization, angiogenesis, cd93, cell adhesion
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 26441.73

Authors

Tassone, G.,Barbera, S.,Raucci, L.,Orlandini, M.,Pozzi, C. (deposition date: 2022-06-14, release date: 2022-11-02, Last modification date: 2024-10-16)

Primary citation

Barbera, S.,Raucci, L.,Tassone, G.,Tinti, L.,Prischi, F.,Santucci, A.,Mongiat, M.,Tosi, G.M.,Galvagni, F.,Dimberg, A.,Pozzi, C.,Orlandini, M.
Dimerization of the C-type lectin-like receptor CD93 promotes its binding to Multimerin-2 in endothelial cells.
Int.J.Biol.Macromol., 224:453-464, 2023

PubMed Abstract: Blocking the signaling activated by the plasma membrane receptor CD93 has recently been demonstrated a useful tool in antiangiogenic treatment and oncotherapy. In the proliferating endothelium, CD93 regulates cell adhesion, migration, and vascular maturation, yet it is unclear how CD93 interacts with the extracellular matrix activating signaling pathways involved in the vascular remodeling. Here for the first time we show that in endothelial cells CD93 is structured as a dimer and that this oligomeric form is physiologically instrumental for the binding of CD93 to its ligand Multimerin-2. Crystallographic X-ray analysis of recombinant CD93 reveals the crucial role played by the C-type lectin-like and sushi-like domains in arranging as an antiparallel dimer to achieve a functional binding state, providing key information for the future design of new drugs able to hamper CD93 function in neovascular pathologies.

PubMed: 36265539
DOI: 10.1016/j.ijbiomac.2022.10.136

Experimental method

X-RAY DIFFRACTION (1.92 Å)