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

The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1). / Davies, Sarah M.A.; Harroun, Thad A.; Hauß, Thomas; Kelly, Sharon M.; Bradshaw, Jeremy P.

In: FEBS Letters, Vol. 548, No. 1-3, 31.07.2003, p. 119-124.

Research output: Contribution to journalArticle

Davies, Sarah M.A. ; Harroun, Thad A. ; Hauß, Thomas ; Kelly, Sharon M. ; Bradshaw, Jeremy P. / The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1). In: FEBS Letters. 2003 ; Vol. 548, No. 1-3. pp. 119-124.
@article{9696c57c3ee24216ba8c0b460b4a82fe,
title = "The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)",
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.",
keywords = "Adenosine diphosphate ribosylation factor, Circular dichroism, Membrane, Neutron diffraction, Phospholipid",
author = "Davies, {Sarah M.A.} and Harroun, {Thad A.} and Thomas Hau{\ss} and Kelly, {Sharon M.} and Bradshaw, {Jeremy P.}",
year = "2003",
month = "7",
day = "31",
doi = "10.1016/S0014-5793(03)00638-0",
language = "English",
volume = "548",
pages = "119--124",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "1-3",

}

TY - JOUR

T1 - The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)

AU - Davies, Sarah M.A.

AU - Harroun, Thad A.

AU - Hauß, Thomas

AU - Kelly, Sharon M.

AU - Bradshaw, Jeremy P.

PY - 2003/7/31

Y1 - 2003/7/31

N2 - 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.

AB - 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.

KW - Adenosine diphosphate ribosylation factor

KW - Circular dichroism

KW - Membrane

KW - Neutron diffraction

KW - Phospholipid

UR - http://www.scopus.com/inward/record.url?scp=0043238695&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)00638-0

DO - 10.1016/S0014-5793(03)00638-0

M3 - Article

VL - 548

SP - 119

EP - 124

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-3

ER -