The membrane bound N‐terminal domain of human adenosine diphosphate ribosylation factor‐1 (ARF1)
- 8 July 2003
- journal article
- Published by Wiley in FEBS Letters
- Vol. 548 (1-3), 119-124
- https://doi.org/10.1016/s0014-5793(03)00638-0
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.Keywords
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