2npr | pdb_00002npr
Structural Studies on Plasmodium vivax Merozoite Surface Protein-1
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Overview
Plasmodium vivax infection is the second most common cause of malaria, throughout the world. Like other Plasmodium species, P. vivax has a large, protein complex, MSP-1, located on the merozoite surface. The C-terminal, MSP-1 sub-unit, MSP-1(42), is cleaved during red blood cell invasion, causing the majority of the complex to be shed and leaving only a small, 15kDa sub-unit, MSP-1(19), on the merozite surface. MSP-1(19) is, considered a strong vaccine candidate. We have determined the solution, structure of MSP-1(19) from P. vivax using nuclear magnetic resonance, (NMR) and show that, like in other Plasmodium species, it consists of two, EGF-like domains that are oriented head-to-tail. The protein has a flat, disk-like shape with a highly charged surface. When MSP-1(19) is part of, the larger MSP-1(42) precursor it exists as an independent domain with no, stable contacts to the rest of the sub-unit. Gel filtration and analytical, ultracentrifugation experiments indicate that P. vivax MSP-1(42) exists as, a dimer in solution. MSP-1(19) itself is a monomer, however, 35, amino-acids immediately upstream of its N-terminus are sufficient to cause, dimerization. Our data suggest that if MSP-1(42) exists as a dimer in, vivo, secondary processing would cause the dissociation of two tightly, linked MSP-1(19) proteins on the merozoite surface just prior to invasion.
About this Structure
2NPR is a Single protein structure of sequence from Plasmodium vivax. Full crystallographic information is available from OCA.
Reference
Structural studies on Plasmodium vivax merozoite surface protein-1., Babon JJ, Morgan WD, Kelly G, Eccleston JF, Feeney J, Holder AA, Mol Biochem Parasitol. 2007 Jan 30;. PMID:17343930
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