C-TERMINAL MEROZOITE SURFACE PROTEIN 1 FROM PLASMODIUM CYNOMOLGIC-TERMINAL MEROZOITE SURFACE PROTEIN 1 FROM PLASMODIUM CYNOMOLGI

Structural highlights

1b9w is a 1 chain structure with sequence from Plasmodium cynomolgi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q25659_9APIC

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The C-terminal proteolytic processing product of merozoite surface protein 1 (MSP1) appears essential for successful erythrocyte invasion by the malarial parasite, Plasmodium. We have determined the crystal structure at 1.8 A resolution of a soluble baculovirus-recombinant form of the protein from P. cynomolgi, which confers excellent protective efficacy in primate vaccination trials. The structure comprises two EGF-like domains, and sequence comparisons strongly suggest that the same conformation is present in all species of Plasmodium, including P. falciparum and P. vivax, which are pathogenic in man. In particular, conserved interdomain contacts between the two EGF modules should preserve the compact form of the molecule in all species. Implications of the crystal structure for anti-malarial vaccine development are discussed.

The crystal structure of C-terminal merozoite surface protein 1 at 1.8 A resolution, a highly protective malaria vaccine candidate.,Chitarra V, Holm I, Bentley GA, Petres S, Longacre S Mol Cell. 1999 Apr;3(4):457-64. PMID:10230398[1]

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

References

  1. Chitarra V, Holm I, Bentley GA, Petres S, Longacre S. The crystal structure of C-terminal merozoite surface protein 1 at 1.8 A resolution, a highly protective malaria vaccine candidate. Mol Cell. 1999 Apr;3(4):457-64. PMID:10230398

1b9w, resolution 1.80Å

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