5tih

Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA

spinqualitylabelsall models 5tih, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tih is a 3 chain structure with sequence from Lk3 transgenic mice and Plaf7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT Related: 5tik Gene: PF3D7_0423800 (PLAF7) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Plasmodium falciparum causes malaria in humans with over 450,000 deaths annually. The asexual blood stage involves invasion of erythrocytes by merozoites, in which they grow and divide to release daughter merozoites, which in turn invade new erythrocytes perpetuating the cycle responsible for malaria. A key step in merozoite invasion is the essential binding of PfRh5/CyRPA/PfRipr complex to basigin, a step linked to formation of a pore between merozoites and erythrocytes. We show CyRPA interacts directly with PfRh5. An invasion inhibitory monoclonal antibody to CyRPA blocks binding of CyRPA to PfRh5 and complex formation thus illuminating the molecular mechanism for inhibition of parasite growth. We determined the crystal structures of CyRPA alone and in complex with antibody Fab fragment. CyRPA has a six-bladed beta-propeller fold, and we identify the region that interacts with PfRh5. This functionally conserved epitope is a potential target for vaccines against P. falciparum. Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA.,Chen L, Xu Y, Wong W, Thompson JK, Healer J, Goddard-Borger E, Lawrence MC, Cowman AF Elife. 2017 Feb 14;6. pii: e21347. doi: 10.7554/eLife.21347. PMID:28195530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody 3D structures

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