2npr

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[[Image:2npr.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2npr", creates the "Structure Box" on the page.
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|GENE= Msp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5855 Plasmodium vivax])
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{{STRUCTURE_2npr| PDB=2npr | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2npr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2npr OCA], [http://www.ebi.ac.uk/pdbsum/2npr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2npr RCSB]</span>
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'''Structural Studies on Plasmodium vivax Merozoite Surface Protein-1'''
'''Structural Studies on Plasmodium vivax Merozoite Surface Protein-1'''
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[[Category: Kelly, G.]]
[[Category: Kelly, G.]]
[[Category: Morgan, W D.]]
[[Category: Morgan, W D.]]
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[[Category: egf-like domain]]
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[[Category: Egf-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:45:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:06:32 2008''
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Revision as of 06:45, 4 May 2008

Template:STRUCTURE 2npr

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 Page seeded by OCA on Sun May 4 09:45:16 2008

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