2npr: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2npr.gif|left|200px]] | [[Image:2npr.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2npr", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_2npr| PDB=2npr | SCENE= }} | |||
| | |||
}} | |||
'''Structural Studies on Plasmodium vivax Merozoite Surface Protein-1''' | '''Structural Studies on Plasmodium vivax Merozoite Surface Protein-1''' | ||
| Line 31: | Line 28: | ||
[[Category: Kelly, G.]] | [[Category: Kelly, G.]] | ||
[[Category: Morgan, W D.]] | [[Category: Morgan, W D.]] | ||
[[Category: | [[Category: Egf-like domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:45:16 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 06:45, 4 May 2008
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
