A structural study of the myristoylated N-terminus of ARF1

  1. Get@NRC: A structural study of the myristoylated N-terminus of ARF1 (Opens in a new window)
DOIResolve DOI: http://doi.org/10.1016/j.bbamem.2004.12.003
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Journal titleBiochimica et biophysica acta. Biomembranes
Pages138144; # of pages: 7
SubjectADP ribosylation factor (ARF); Myristoylation; Neutron diffraction; Phospholipid
AbstractThe effect of myristoylation on the 15-amino-acid peptide from the membrane-binding N-terminus of ADP ribosylation factor 1 (ARF1) was studied using neutron diffraction and circular dichroism. A previous study on the non-acylated form indicated that the peptide lies parallel to the membrane, at a shallow depth and in the vicinity of the phosphorylcholine headgroups. It was suggested that the helix does not extend past residue 12, an important consequence for the linking region of the ARF1 protein. In this paper, we show that the result of myristoylation is to increase the helical content reaching the peptide's C-terminus, resulting in the formation of a new hydrophobic face. This increased helicity may augment the entire protein's membrane-binding affinity, indicating that ARF1 effectively has two interdependent membrane-binding motifs.
Publication date
AffiliationNational Research Council Canada; NRC Canadian Neutron Beam Centre
Peer reviewedNo
NPARC number12338482
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Record identifierb925038a-498c-4cb2-87b3-133d96ad45e7
Record created2009-09-10
Record modified2016-05-09
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