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

Download
  1. Get@NRC: The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1) (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1016/S0014-5793(03)00638-0
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeArticle
Journal titleFEBS Letters
Volume548
Issue1-3
Pages119124; # of pages: 6
SubjectAdenosine diphosphate ribosylation factor; Circular dichroism; Membrane; Neutron diffraction; Phospholipid
AbstractThe 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.
Publication date
LanguageEnglish
Peer reviewedNo
NRC publication
This is a non-NRC publication

"Non-NRC publications" are publications authored by NRC employees prior to their employment by NRC.

NPARC number12334534
Export citationExport as RIS
Report a correctionReport a correction
Record identifier3845814d-f214-483a-974e-22c8f3fb22d5
Record created2009-09-10
Record modified2016-05-09
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)