A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease.
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.
Freund
J
J
Max-Planck-Institute for Medical Research, Department of Biophysics, Heidelberg, Germany.
Kellner
R
R
Konvalinka
J
J
Wolber
V
V
Kräusslich
H G
HG
Kalbitzer
H R
HR
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression / Q000235:genetics; D015693:Gene Products, nef / Q000737:chemistry / Q000378:metabolism*; D016333:HIV Protease / Q000378:metabolism*; D015497:HIV-1 / Q000737:chemistry / Q000378:metabolism*; D015498:HIV-2 / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017510:Protein Folding; D015302:Simian Immunodeficiency Virus / Q000737:chemistry; D054311:nef Gene Products, Human Immunodeficiency Virus
D015693:Gene Products, nef; D054311:nef Gene Products, Human Immunodeficiency Virus; D016333:HIV Protease