8C3Y
HB3VAR03 apo headstructure (PfEMP1 A)
Summary for 8C3Y
| Entry DOI | 10.2210/pdb8c3y/pdb |
| EMDB information | 16415 |
| Descriptor | PfEMP1 (1 entity in total) |
| Functional Keywords | plasmodium falciparum, cerebral malaria, pfemp1, epcr, cell adhesion |
| Biological source | Plasmodium falciparum HB3 |
| Total number of polymer chains | 1 |
| Total formula weight | 145128.73 |
| Authors | Raghavan, S.S.R.,Lavstsen, T.,Wang, K.T. (deposition date: 2022-12-29, release date: 2023-08-02, Last modification date: 2024-10-09) |
| Primary citation | Rajan Raghavan, S.S.,Turner, L.,Jensen, R.W.,Johansen, N.T.,Jensen, D.S.,Gourdon, P.,Zhang, J.,Wang, Y.,Theander, T.G.,Wang, K.,Lavstsen, T. Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1. Structure, 31:1174-1183.e4, 2023 Cited by PubMed Abstract: 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 CIDRα1 domains interact with the adjacent DBLα1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLα1 domain is displaced, and the EPCR-binding helix of CIDRα1 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. PubMed: 37582356DOI: 10.1016/j.str.2023.07.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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