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 journalArticle

6 Citations (Scopus)

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

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