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The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)
Sarah M A Davies1, Thad A Harroun, Thomas Hauss
1Department of Preclinical Veterinary Sciences, R.(D.)S.V.S., University of Edinburgh, Summerhall, Edinburgh, EH9 1QH, UK.
Abstract:
The small G protein adenosine diphosphate ribosylation factor-1 (ARF1) is activated by cell membrane binding of a self-folding N-terminal domain. We present a model of the human ARF1 N-terminal peptide in planar lipid bilayers, determined from neutron lamellar diffraction and circular dichroism data with molecular modelling. This amphipathic domain lies at a shallow membrane depth, ideal for regulation of the ARF1 bio-timer by rapid, reversible membrane binding. The helical region does not elongate upon membrane binding, leaving the connecting flexible linker region's length unchanged.
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