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2npr
From Proteopedia
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| - | [[Image:2npr.gif|left|200px]] | ||
| - | + | ==Structural Studies on Plasmodium vivax Merozoite Surface Protein-1== | |
| - | + | <StructureSection load='2npr' size='340' side='right'caption='[[2npr]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2npr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax_strain_Belem Plasmodium vivax strain Belem]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NPR FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2npr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2npr OCA], [https://pdbe.org/2npr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2npr RCSB], [https://www.ebi.ac.uk/pdbsum/2npr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2npr ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | | | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/Q8I1L1_PLAVI Q8I1L1_PLAVI] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/np/2npr_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2npr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:17343930</ref> | |
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| - | Structural studies on Plasmodium vivax merozoite surface protein-1., Babon JJ, Morgan WD, Kelly G, Eccleston JF, Feeney J, Holder AA | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2npr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Plasmodium vivax strain Belem]] | ||
| + | [[Category: Babon JJ]] | ||
| + | [[Category: Eccleston JF]] | ||
| + | [[Category: Feeney J]] | ||
| + | [[Category: Holder AA]] | ||
| + | [[Category: Kelly G]] | ||
| + | [[Category: Morgan WD]] | ||
Current revision
Structural Studies on Plasmodium vivax Merozoite Surface Protein-1
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