Residues belonging the n-terminal region derived of merozoite surface protein-2 of plasmodium falciparumResidues belonging the n-terminal region derived of merozoite surface protein-2 of plasmodium falciparum

Structural highlights

2mu8 is a 1 chain structure with sequence from Plasmodium falciparum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MSA2_PLAF7 May play a role in the merozoite attachment to the erythrocyte.

Publication Abstract from PubMed

The conserved, nonantigenic, nonimmunogenic malaria Merozoite Surface Protein-2 peptide 1, having high affinity for red blood cells, was rendered immunogenic and protective in Aotus monkeys by specifically changing some critical residues. The NMR structure revealed a switch from classical type III' into distorted III' and III beta turns in the protective peptides. These changes may lead to a better fit into the Aotus MHC class II human HLA-DRbeta1 12 molecule equivalent, thus activating the immune system.

Distorting malaria peptide backbone structure to enable fitting into MHC class II molecules renders modified peptides immunogenic and protective.,Cifuentes G, Patarroyo ME, Urquiza M, Ramirez LE, Reyes C, Rodriguez R J Med Chem. 2003 May 22;46(11):2250-3. PMID:12747797[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Cifuentes G, Patarroyo ME, Urquiza M, Ramirez LE, Reyes C, Rodriguez R. Distorting malaria peptide backbone structure to enable fitting into MHC class II molecules renders modified peptides immunogenic and protective. J Med Chem. 2003 May 22;46(11):2250-3. PMID:12747797 doi:http://dx.doi.org/10.1021/jm020440w
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