Nef protein of human immunodeficiency virus type 1 binds its own myristoylated N-terminus

Hoffmann, S.; Jonas, E.; König, S.; Preusser-Kunze, A.; Willbold, D.

doi:10.1515/BC.2007.020

Journal Article

PreJuSER-55895

Nef protein of human immunodeficiency virus type 1 binds its own myristoylated N-terminus

Hoffmann, S.FZJ* ; Jonas, E.FZJ* ; König, S. ; Preusser-Kunze, A. ; Willbold, D.FZJ*

2007
de Gruyter Berlin [u.a.]

Biological chemistry 388, 181 - 183 (2007) [10.1515/BC.2007.020]

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Please use a persistent id in citations: http://hdl.handle.net/2128/18356 doi:10.1515/BC.2007.020

Abstract: 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.

Keyword(s): Calorimetry: methods (MeSH) ; Gene Products, nef: chemistry (MeSH) ; Humans (MeSH) ; Myristic Acid: chemistry (MeSH) ; Peptides: chemistry (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Spectrometry, Fluorescence (MeSH) ; nef Gene Products, Human Immunodeficiency Virus (MeSH) ; Gene Products, nef ; Peptides ; Recombinant Proteins ; nef Gene Products, Human Immunodeficiency Virus ; Myristic Acid ; J ; fluorescence titration (auto) ; peptide binding (auto) ; protein conformation (auto)