Document 0320
 DOCN  M9460320
 TI    Stability and proteolytic domains of Nef protein from human
       immunodeficiency virus (HIV) type 1.
 DT    9408
 AU    Freund J; Kellner R; Houthaeve T; Kalbitzer HR; Max-Planck-Institute for
       Medical Research, Department of; Biophysics, Heidelberg, Germany.
 SO    Eur J Biochem. 1994 Apr 15;221(2):811-9. Unique Identifier : AIDSLINE
       MED/94229079
 AB    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.
 DE    Amino Acid Sequence  Electrophoresis, Polyacrylamide Gel  Escherichia
       coli/GENETICS  Gene Products, nef/*CHEMISTRY/GENETICS/METABOLISM
       Histidine/METABOLISM  Human  Hydrogen-Ion Concentration  HIV
       Protease/METABOLISM  HIV-1/*CHEMISTRY/GENETICS  Molecular Sequence Data
       Nuclear Magnetic Resonance  Pancreatopeptidase/METABOLISM  Protein
       Denaturation  Solubility  Support, Non-U.S. Gov't  Temperature
       Trypsin/METABOLISM  Tyrosine/METABOLISM  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).