The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)

Sarah M.A. Davies, Thad A. Harroun, Thomas Hauß, Sharon M. Kelly, Jeremy P. Bradshaw

Research output: Contribution to journalArticlepeer-review

6 Citations (SciVal)

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 languageEnglish
Pages (from-to)119-124
Number of pages6
JournalFEBS Letters
Volume548
Issue number1-3
DOIs
Publication statusPublished - 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

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