%0 Journal Article
%A Hoffmann, S.
%A Jonas, E.
%A König, S.
%A Preusser-Kunze, A.
%A Willbold, D.
%T Nef protein of human immunodeficiency virus type 1 binds its own myristoylated N-terminus
%J Biological chemistry
%V 388
%@ 1431-6730
%C Berlin [u.a.]
%I de Gruyter
%M PreJuSER-55895
%P 181 - 183
%D 2007
%Z Record converted from VDB: 12.11.2012
%X HIV-1 Nef is a small protein (approx. 25 kDa) that is posttranslationally modified by myristoylation. To explain its complex activities, a 'Nef-cycle' is discussed, which postulates different molecular conformations of Nef. Using recombinant full-length non-myristoylated Nef and synthetic peptides, we demonstrate by fluorescence titration experiments that a peptide representing the myristoylated N-terminus of Nef is specifically bound by Nef. A non-myristoylated N-terminal fragment of Nef or a myristoylated control peptide does not bind to Nef. These results are the first direct experimental evidence of the existence of a myristate-binding pocket in Nef, a prerequisite of the postulated 'closed' Nef conformation.
%K Calorimetry: methods
%K Gene Products, nef: chemistry
%K Humans
%K Myristic Acid: chemistry
%K Peptides: chemistry
%K Recombinant Proteins: chemistry
%K Spectrometry, Fluorescence
%K nef Gene Products, Human Immunodeficiency Virus
%K Gene Products, nef (NLM Chemicals)
%K Peptides (NLM Chemicals)
%K Recombinant Proteins (NLM Chemicals)
%K nef Gene Products, Human Immunodeficiency Virus (NLM Chemicals)
%K Myristic Acid (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:17261081
%U <Go to ISI:>//WOS:000243978600006
%R 10.1515/BC.2007.020
%U https://juser.fz-juelich.de/record/55895