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

doi:10.1016/S0014-5793(03)00638-0

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 journal › Article › peer-review

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 language	English
Pages (from-to)	119-124
Number of pages	6
Journal	FEBS Letters
Volume	548
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00638-0
Publication status	Published - 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

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10.1016/S0014-5793(03)00638-0

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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.",

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AU - Davies, Sarah M.A.

AU - Harroun, Thad A.

AU - Hauß, Thomas

AU - Kelly, Sharon M.

AU - Bradshaw, Jeremy P.

PY - 2003/7/31

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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

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