3lrp
Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1
Structural highlights
Function[ARF1_PLAFA] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity). Publication Abstract from PubMedVesicular trafficking may play a crucial role in the pathogenesis and survival of the malaria parasite. ADP-ribosylation factors (ARFs) are among the major components of vesicular trafficking pathways in eukaryotes. The crystal structure of ARF1 GTPase from Plasmodium falciparum has been determined in the GDP-bound conformation at 2.5 A resolution and is compared with the structures of mammalian ARF1s. Structure of Plasmodium falciparum ADP-ribosylation factor 1.,Cook WJ, Smith CD, Senkovich O, Holder AA, Chattopadhyay D Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1426-31. Epub 2010 Oct 27. PMID:21045287[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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