Structural highlights
FunctionC1QR1_HUMAN Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion. Publication Abstract from PubMedBlocking 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. Dimerization of the C-type lectin-like receptor CD93 promotes its binding to Multimerin-2 in endothelial cells.,Barbera S, Raucci L, Tassone G, Tinti L, Prischi F, Santucci A, Mongiat M, Tosi GM, Galvagni F, Dimberg A, Pozzi C, Orlandini M Int J Biol Macromol. 2022 Oct 18. pii: S0141-8130(22)02378-9. doi:, 10.1016/j.ijbiomac.2022.10.136. PMID:36265539[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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