Premium
The membrane bound N‐terminal domain of human adenosine diphosphate ribosylation factor‐1 (ARF1)
Author(s) -
Davies Sarah M.A,
Harroun Thad A,
Hauß Thomas,
Kelly Sharon M,
Bradshaw Jeremy P
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00638-0
Subject(s) - adp ribosylation factor , biophysics , membrane , chemistry , linker , crystallography , helix (gastropod) , biochemistry , cell , biology , ecology , snail , computer science , golgi apparatus , operating system
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.