Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Structure of Plasmodium falciparum ADP-ribosylation factor 1

Journal Article · · Acta Crystallogr. F
Vesicular 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 {angstrom} resolution and is compared with the structures of mammalian ARF1s.
Research Organization:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Organization:
DOE - BASIC ENERGY SCIENCES
OSTI ID:
1025631
Journal Information:
Acta Crystallogr. F, Journal Name: Acta Crystallogr. F Journal Issue: (11) ; 11, 2010 Vol. 66; ISSN 1744-3091
Country of Publication:
United States
Language:
ENGLISH

Similar Records

Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP)
Journal Article · Mon Mar 26 00:00:00 EDT 2012 · Acta Crystallogr. F · OSTI ID:1034548

Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene
Journal Article · Thu May 01 00:00:00 EDT 1997 · Genomics · OSTI ID:530749

Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively
Journal Article · Sat Jun 01 00:00:00 EDT 1996 · Genomics · OSTI ID:476792