Overproduction, purification and crystallization of a chondroitin sulfate A-binding DBL domain from a Plasmodium falciparum var2csa-encoded PfEMP1 protein.
In: Acta crystallographica. Section F, Structural biology and crystallization communications, Jg. 64 (2008-03-01), Heft Pt 3, S. 221-3
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Zugriff:
The PfEMP1 proteins of the malaria parasite Plasmodium falciparum are inserted into the membrane of infected red blood cells, where they mediate adhesion to a variety of human receptors. The DBL domains of the var2csa-encoded PfEMP1 protein play a critical role in malaria of pregnancy, tethering infected cells to the surface of the placenta through interactions with the glycosaminoglycan carbohydrate chondroitin sulfate A (CSA). A CSA-binding DBL domain has been overproduced in a bacterial expression system, purified and crystallized. Native data sets extending to 1.9 A resolution have been collected and phasing is under way.
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Overproduction, purification and crystallization of a chondroitin sulfate A-binding DBL domain from a Plasmodium falciparum var2csa-encoded PfEMP1 protein.
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Autor/in / Beteiligte Person: | Higgins, MK |
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Zeitschrift: | Acta crystallographica. Section F, Structural biology and crystallization communications, Jg. 64 (2008-03-01), Heft Pt 3, S. 221-3 |
Veröffentlichung: | Oxford, England : Wiley-Blackwell ; <i>Original Publication</i>: Chester, England : International Union of Crystallography, c2005-, 2008 |
Medientyp: | academicJournal |
ISSN: | 1744-3091 (electronic) |
DOI: | 10.1107/S1744309108004211 |
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