Abstract:
:Nef is an HIV-1 accessory protein that directly contributes to AIDS progression. Nef is myristoylated on the N-terminus, associates with membranes, and may undergo a transition from a solution conformation to a membrane-associated conformation. It has been hypothesized that conformational rearrangement enables membrane-associated Nef to interact with cellular proteins. Despite its medical relevance, to our knowledge there is no direct information about the conformation of membrane-bound Nef. In this work, we used neutron reflection to reveal what we believe are the first details of the conformation of membrane-bound Nef. The conformation of Nef was probed upon binding to Langmuir monolayers through the interaction of an N-terminal His tag with a synthetic metal-chelating lipid, which models one of the possible limiting cases for myr-Nef. The data indicate that residues are inserted into the lipid headgroups during interaction, and that the core domain lies directly against the lipid headgroups, with a thickness of ∼40 A. Binding of Nef through the N-terminal His tag apparently facilitates insertion of residues, as no insertion occurred upon binding of Nef through weak electrostatic interactions in the absence of the specific interaction through the His tag.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Kent MS,Murton JK,Sasaki DY,Satija S,Akgun B,Nanda H,Curtis JE,Majewski J,Morgan CR,Engen JRdoi
10.1016/j.bpj.2010.07.016subject
Has Abstractpub_date
2010-09-22 00:00:00pages
1940-8issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(10)00861-1journal_volume
99pub_type
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