2npr: Difference between revisions
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[[Image:2npr.gif|left|200px]] | [[Image:2npr.gif|left|200px]] | ||
'''Structural Studies on Plasmodium vivax Merozoite Surface Protein-1''' | {{Structure | ||
|PDB= 2npr |SIZE=350|CAPTION= <scene name='initialview01'>2npr</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= Msp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5855 Plasmodium vivax]) | |||
}} | |||
'''Structural Studies on Plasmodium vivax Merozoite Surface Protein-1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NPR is a [ | 2NPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPR OCA]. | ||
==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 May;153(1):31-40. Epub 2007 Jan 30. PMID:[http:// | 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://www.ncbi.nlm.nih.gov/pubmed/17343930 17343930] | ||
[[Category: Plasmodium vivax]] | [[Category: Plasmodium vivax]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: egf-like domain]] | [[Category: egf-like domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:49:27 2008'' | ||
Revision as of 15:49, 20 March 2008
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| Gene: | Msp1 (Plasmodium vivax) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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