2NPR
Structural Studies on Plasmodium vivax Merozoite Surface Protein-1
Summary for 2NPR
| Entry DOI | 10.2210/pdb2npr/pdb |
| NMR Information | BMRB: 15007 |
| Descriptor | Merozoite surface protein 1 (1 entity in total) |
| Functional Keywords | egf-like domain, membrane protein |
| Biological source | Plasmodium vivax (strain Belem) |
| Total number of polymer chains | 1 |
| Total formula weight | 9823.01 |
| Authors | Babon, J.J.,Morgan, W.D.,Kelly, G.,Eccleston, J.F.,Feeney, J.,Holder, A.A. (deposition date: 2006-10-29, release date: 2007-03-20, Last modification date: 2024-11-13) |
| Primary citation | Babon, J.J.,Morgan, W.D.,Kelly, G.,Eccleston, J.F.,Feeney, J.,Holder, A.A. Structural studies on Plasmodium vivax merozoite surface protein-1 Mol.Biochem.Parasitol., 153:31-40, 2007 Cited by PubMed Abstract: 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. PubMed: 17343930DOI: 10.1016/j.molbiopara.2007.01.015 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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