1n1i

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spinqualitylabelsall models 1n1i, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The structure of MSP-1(19) from Plasmodium knowlesi

Overview

The protozoan parasite Plasmodium causes malaria, with hundreds of, millions of cases recorded annually. Protection against malaria infection, can be conferred by antibodies against merozoite surface protein (MSP)-1, making it an attractive vaccine candidate. Here we present the structure, of the C-terminal domains of MSP-1 (known as MSP-1(19)) from Plasmodium, knowlesi. The structure reveals two tightly packed epidermal growth, factor-like domains oriented head to tail. In domain 1, the molecule, displays a histidine binding site formed primarily by a highly conserved, tryptophan. The protein carries a pronounced overall negative charge, primarily due to the large number of acidic groups in domain 2. To map, protein binding surfaces on MSP-1(19), we have analyzed the crystal, contacts in five different crystal environments, revealing that domain 1, is highly preferred in protein-protein interactions. A comparison of, MSP-1(19) structures from P. knowlesi, P. cynomolgi, and P. falciparum, shows that, although the overall protein folds are similar, the molecules, show significant differences in charge distribution. We propose the, histidine binding site in domain 1 as a target for inhibitors of protein, binding to MSP-1, which might prevent invasion of the merozoite into red, blood cells.

About this Structure

1N1I is a Single protein structure of sequence from Plasmodium knowlesi with IMD and HIS as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the C-terminal domains of merozoite surface protein-1 from Plasmodium knowlesi reveals a novel histidine binding site., Garman SC, Simcoke WN, Stowers AW, Garboczi DN, J Biol Chem. 2003 Feb 28;278(9):7264-9. Epub 2002 Dec 19. PMID:12493733

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