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 |
Funding
We thank Thomas Gutberlet and Silvia Dante for expert technical assistance with V1 at the HMI, Nicholas Price and the BBSRC for access to the Scottish Circular Dichroism centre. Support for use of the BENSC facilities at the HMI was provided by the European Commission, under the Human Potential Programme’s Access to Research Infrastructures action. S.M.A.D. was a Wellcome Trust International Fellow.
Keywords
- Adenosine diphosphate ribosylation factor
- Circular dichroism
- Membrane
- Neutron diffraction
- Phospholipid
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology