4p1t

Crystal structure of the DBL3X-DBL4epsilon double domain from the extracellular part of VAR2CSA PfEMP1 from Plasmodium falciparum

spinqualitylabelsall models 4p1t, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p1t is a 1 chain structure with sequence from Plasmodium falciparum FCR-3/Gambia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6UDW7_PLAFA Publication Abstract from PubMed The human malaria parasite, Plasmodium falciparum, is able to evade spleen-mediated clearing from blood stream by sequestering in peripheral organs. This is due to the adhesive properties conferred by the P. falciparum Erythrocyte Membrane Protein 1 (PfEMP1) family exported by the parasite to the surface of infected erythrocytes. Expression of the VAR2CSA variant of PfEMP1 leads to pregnancy-associated malaria, which occurs when infected erythrocytes massively sequester in the placenta by binding to low-sulfated Chondroitin Sulfate A (CSA) present in the intervillous spaces. VAR2CSA is a 350 kDa protein that carries six Duffy-Binding Like (DBL) domains, one Cysteine-rich Inter-Domain Regions (CIDR) and several inter-domain regions. In the present paper, we report for the first time the crystal structure at 2.9 A of a VAR2CSA double domain, DBL3X-DBL4epsilon, from the FCR3 strain. DBL3X and DBL4epsilon share a large contact interface formed by residues that are invariant or highly conserved in VAR2CSA variants, which suggests that these two central DBL domains (DBL3X-DBL4epsilon) contribute significantly to the structuring of the functional VAR2CSA extracellular region. We have also examined the antigenicity of peptides corresponding to exposed loop regions of the DBL4epsilon structure. Structure of the DBL3X-DBL4epsilon region of the VAR2CSA placental malaria vaccine candidate: insight into DBL domain interactions.,Gangnard S, Lewit-Bentley A, Dechavanne S, Srivastava A, Amirat F, Bentley GA, Gamain B Sci Rep. 2015 Oct 9;5:14868. doi: 10.1038/srep14868. PMID:26450557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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