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  Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1

Freund, J., Kellner, R., Houthaeve, T., & Kalbitzer, H. R. (1994). Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1. European Journal of Biochemistry, 221(2), 811-819. doi:10.1111/j.1432-1033.1994.tb18795.x.

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EurJBiochem_221_1994_811.pdf (beliebiger Volltext), 961KB
 
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 Urheber:
Freund, Jens1, Autor           
Kellner, Roland, Autor
Houthaeve, Tony, Autor
Kalbitzer, Hans Robert1, Autor           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Zusammenfassung: Proteolytic experiments in conjunction with 1H-NMR spectroscopy show that the Nef (negative factor) protein from human immunodeficiency virus type 1 probably consists of two main domains, the N-terminal anchor domain at amino acid positions 2-65 and the C-terminal core domain at positions 66-206. The N-terminal domain is likely to be located at the surface of the protein, while the C-terminal domain has a compactly folded core and is stable in the absence of the anchor domain. It is conceivable that the core domain represents a functional domain of the Nef protein, activated after the removal of the membrane anchor by the human-immunodeficiency-virus protease or cellular proteases. Nef is stable at pH 5-12 and denatures at 317-322 K. The Nef protein remains in its native conformation in dimethyl-sulfoxide/water mixtures up to 35% (by vol.), and in acetonitrile/water up to 14% (by vol.). Nef refolds spontaneously after denaturation with urea or guanidinium hydrochloride. The 1H-NMR parameters and pKa values of five of the nine histidine residues and one of the seven tyrosine residues were determined and were found in four cases to be typical for residues which are not located in the interior of the protein.

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Sprache(n): eng - English
 Datum: 1993-12-211994-02-222005-03-031994-04
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 665171
DOI: 10.1111/j.1432-1033.1994.tb18795.x
URI: http://www.ncbi.nlm.nih.gov/pubmed/8174561
Anderer: 6898
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Titel: European Journal of Biochemistry
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Seiten: - Band / Heft: 221 (2) Artikelnummer: - Start- / Endseite: 811 - 819 Identifikator: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040