ARF3 Human

ARF3 is a small guanine nucleotide-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase . This protein is involved in protein trafficking and may modulate vesicle budding and uncoating within the Golgi apparatus . ARF3 proteins cycle between inactive GDP-bound and active GTP-bound forms, which bind selectively to effectors .

The classical structural GDP/GTP switch in ARF3 is characterized by conformational changes at the switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide . In the GTP-bound form, ARF3 undergoes a conformational change that affects the beta2beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N-terminus . This conformational change is crucial for its function in vesicular trafficking and actin remodeling.

Recombinant human ARF3 protein, fused to a His-tag at the N-terminus, is expressed in E. coli and purified using conventional chromatography . This recombinant protein is used in various research applications to study the function and mechanism of ARF3 in cellular processes.

ARF3 is used in research to understand its role in vesicular trafficking, protein trafficking, and its interaction with other proteins involved in these processes . It is also studied for its potential implications in diseases where protein trafficking is disrupted.