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 |
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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