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2flg
From Proteopedia
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|PDB= 2flg |SIZE=350|CAPTION= <scene name='initialview01'>2flg</scene> | |PDB= 2flg |SIZE=350|CAPTION= <scene name='initialview01'>2flg</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1cej|1CEJ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2flg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2flg OCA], [http://www.ebi.ac.uk/pdbsum/2flg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2flg RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Pluschke, G.]] | [[Category: Pluschke, G.]] | ||
[[Category: Robinson, J.]] | [[Category: Robinson, J.]] | ||
| - | [[Category: NH2]] | ||
[[Category: egf-like domain]] | [[Category: egf-like domain]] | ||
[[Category: extracellular]] | [[Category: extracellular]] | ||
| Line 33: | Line 35: | ||
[[Category: surface protein]] | [[Category: surface protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:04:22 2008'' |
Revision as of 00:04, 31 March 2008
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| Ligands: | |||||||
| Related: | 1CEJ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of an EGF-LIKE domain from the Plasmodium falciparum merozoite surface protein 1
Overview
The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal growth factor), each stabilized by three disulfide bonds. The native conformation of this protein is important for eliciting P. falciparum growth inhibitory antibodies. Here we show that the N-terminal EGF domain alone can be chemically synthesized and efficiently refolded to a native-like state, as shown by its solution structure as determined by NMR spectroscopy. In order to study its immunogenicity, the domain was coupled through its N terminus to a phospholipid and incorporated into reconstituted influenza virus-like particles (virosomes). When used to immunize mice, the peptide-loaded virosomes elicited potent humoral immune responses that were shown by Western blots and immunofluorescence assays to cross-react with native MSP-1 on the surfaces of P. falciparum blood stage parasites. This opens the way for a medicinal chemistry-oriented approach to the study and optimization of the antigenicity of the protein as a potential malaria vaccine candidate, whilst exploiting the immunopotentiating properties of influenza virosomes as a delivery vehicle.
About this Structure
2FLG is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Synthesis, solution structure and immune recognition of an epidermal growth factor-like domain from Plasmodium falciparum merozoite surface protein-1., James S, Moehle K, Renard A, Mueller MS, Vogel D, Zurbriggen R, Pluschke G, Robinson JA, Chembiochem. 2006 Dec;7(12):1943-50. PMID:17068840
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