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

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)119-24
Number of pages6
JournalFEBS Letters
Volume548
Issue number1-3
Publication statusPublished - 2003

Keywords

  • ADP-Ribosylation Factor 1
  • Amino Acid Sequence
  • Circular Dichroism
  • Deuterium
  • Humans
  • Lipid Bilayers/metabolism
  • Membrane Proteins
  • Models, Molecular
  • Neutron Diffraction
  • Protein Structure, Tertiary

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