2npr
From Proteopedia
(New page: 200px<br /><applet load="2npr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2npr" /> '''Structural Studies on Plasmodium vivax Meroz...) |
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==Overview== | ==Overview== | ||
| - | Plasmodium vivax infection is the second most common cause of malaria | + | 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== | ==About this Structure== | ||
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==Reference== | ==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 | + | 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 May;153(1):31-40. Epub 2007 Jan 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17343930 17343930] |
[[Category: Plasmodium vivax]] | [[Category: Plasmodium vivax]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Babon, J | + | [[Category: Babon, J J.]] |
| - | [[Category: Eccleston, J | + | [[Category: Eccleston, J F.]] |
[[Category: Feeney, J.]] | [[Category: Feeney, J.]] | ||
| - | [[Category: Holder, A | + | [[Category: Holder, A A.]] |
[[Category: Kelly, G.]] | [[Category: Kelly, G.]] | ||
| - | [[Category: Morgan, W | + | [[Category: Morgan, W D.]] |
[[Category: egf-like domain]] | [[Category: egf-like domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:32 2008'' |
Revision as of 16:09, 21 February 2008
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Structural Studies on Plasmodium vivax Merozoite Surface Protein-1
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 May;153(1):31-40. Epub 2007 Jan 30. PMID:17343930
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