The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1).
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.
Davies
Sarah M A
SM
Department of Preclinical Veterinary Sciences, R.(D.)S.V.S., University of Edinburgh, Summerhall, Edinburgh, EH9 1QH, UK.
Harroun
Thad A
TA
Hauss
Thomas
T
Kelly
Sharon M
SM
Bradshaw
Jeremy P
JP
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
D008051:Lipid Bilayers; D008565:Membrane Proteins; D003903:Deuterium; D020823:ADP-Ribosylation Factor 1