8c44

HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR

spinqualitylabelsall models 8c44, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8c44 is a 2 chain structure with sequence from Homo sapiens and Plasmodium falciparum HB3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Ligands: NAG, PTY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0L7KL67_PLAFX Publication Abstract from PubMed Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRalpha1 domains interact with the adjacent DBLalpha1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLalpha1 domain is displaced, and the EPCR-binding helix of CIDRalpha1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family. Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1.,Rajan Raghavan SS, Turner L, Jensen RW, Johansen NT, Jensen DS, Gourdon P, Zhang J, Wang Y, Theander TG, Wang K, Lavstsen T Structure. 2023 Oct 5;31(10):1174-1183.e4. doi: 10.1016/j.str.2023.07.011. Epub , 2023 Aug 14. PMID:37582356 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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