6zbh | pdb_00006zbh

Merozoite surface protein 1 (MSP-1) from Plasmodium falciparum, alternative conformation 5

spinqualitylabelsall models 6zbh, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zbh is a 4 chain structure with sequence from Plasmodium falciparum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in Plasmodium infection and immunity. Structure of the merozoite surface protein 1 from Plasmodium falciparum.,Dijkman PM, Marzluf T, Zhang Y, Chang SS, Helm D, Lanzer M, Bujard H, Kudryashev M Sci Adv. 2021 Jun 2;7(23):eabg0465. doi: 10.1126/sciadv.abg0465. Print 2021 Jun. PMID:34078606 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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