The macromolecular complex of ICP and falcipain-2 fromPlasmodium: preparation, crystallization and preliminary X-ray diffraction analysis
| Autor: | Britta Schwarzloh, Annika Rennenberg, Guido Hansen, Rolf Hilgenfeld, Volker Heussler |
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| Rok vydání: | 2011 |
| Předmět: |
Proteases
Plasmodium falciparum Biophysics Cysteine Proteinase Inhibitors Crystallography X-Ray Biochemistry law.invention Structural Biology law parasitic diseases Genetics Crystallization biology Plasmodium (life cycle) Condensed Matter Physics biology.organism_classification Cysteine Endopeptidases Crystallization Communications X-ray crystallography Recombinant DNA Protein Binding Cysteine |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:1406-1410 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309111034592 |
| Popis: | The malaria parasite Plasmodium depends on the tight control of cysteine-protease activity throughout its life cycle. Recently, the characterization of a new class of potent inhibitors of cysteine proteases (ICPs) secreted by Plasmodium has been reported. Here, the recombinant production, purification and crystallization of the inhibitory C-terminal domain of ICP from P. berghei in complex with the P. falciparum haemoglobinase falcipain-2 is described. The 1:1 complex was crystallized in space group P4(3), with unit-cell parameters a = b = 71.15, c = 120.09 Å. A complete diffraction data set was collected to a resolution of 2.6 Å. |
| Databáze: | OpenAIRE |
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