Document 0451
 DOCN  M9490451
 TI    A possible regulation of negative factor (Nef) activity of human
       immunodeficiency virus type 1 by the viral protease.
 DT    9411
 AU    Freund J; Kellner R; Konvalinka J; Wolber V; Krausslich HG; Kalbitzer
       HR; Max-Planck-Institute for Medical Research, Department of;
       Biophysics, Heidelberg, Germany.
 SO    Eur J Biochem. 1994 Jul 15;223(2):589-93. Unique Identifier : AIDSLINE
       GENBANK
 AB    Negative factor (Nef) protein from human immunodeficiency virus type 1
       (HIV-1) is cleaved into two well-defined domains by the HIV-1-encoded
       protease. The cleavage site is located between Trp57 and Leu58 and is
       well conserved. The two domains are stable in the presence of protease
       for more than 48 h. The C-terminal core domain contains a well-conserved
       well-folded region. The cleavage releases the core domain from the
       myristoylated membrane anchor domain. As is the case for other HIV
       proteins, cleavage of Nef could be crucial for correct biological
       function.
 DE    Amino Acid Sequence  Comparative Study  Electrophoresis, Polyacrylamide
       Gel  Escherichia coli/GENETICS  Gene Expression/GENETICS  Gene Products,
       nef/CHEMISTRY/*METABOLISM  Human  HIV Protease/*METABOLISM
       HIV-1/CHEMISTRY/*METABOLISM  HIV-2/CHEMISTRY  Molecular Sequence Data
       Molecular Weight  Protein Folding  Support, Non-U.S. Gov't
       SIV/CHEMISTRY  JOURNAL ARTICLE

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