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.
| Original language | English |
|---|---|
| Pages (from-to) | 119-124 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 548 |
| Issue number | 1-3 |
| DOIs | |
| Publication status | Published - 31 Jul 2003 |
Keywords
- Adenosine diphosphate ribosylation factor
- Circular dichroism
- Membrane
- Neutron diffraction
- Phospholipid
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Davies, S. M. A., Harroun, T. A., Hauß, T., Kelly, S. M., & Bradshaw, J. P. (2003). The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1). FEBS Letters, 548(1-3), 119-124. https://doi.org/10.1016/S0014-5793(03)00638-0