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.
authors.affiliation: Department of Preclinical Veterinary Sciences, R.(D.)S.V.S., University of Edinburgh, Summerhall, Edinburgh, EH9 1QH, UK.
authors.forename: Sarah M A
authors.initials: SM
authors.lastname: Davies
authors.forename: Thad A
authors.initials: TA
authors.lastname: Harroun
authors.forename: Thomas
authors.initials: T
authors.lastname: Hauss
authors.forename: Sharon M
authors.initials: SM
authors.lastname: Kelly
authors.forename: Jeremy P
authors.initials: JP
authors.lastname: Bradshaw
mesh_terms: D020823:ADP-Ribosylation Factor 1 / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003903:Deuterium; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D033363:Neutron Diffraction; D017434:Protein Structure, Tertiary
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins; D003903:Deuterium; D020823:ADP-Ribosylation Factor 1