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

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/S0014-5793(03)00638-0
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FormatText, Article
SubjectAdenosine diphosphate ribosylation factor; Circular dichroism; Membrane; Neutron diffraction; Phospholipid
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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  • FEBS Letters 548, no. 1-3 (31 July 2003): 119–124.
LanguageEnglish
NRC publication
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NPARC number12334534
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Record identifier3845814d-f214-483a-974e-22c8f3fb22d5
Record created2009-09-10
Record modified2020-04-02
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