de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons92960

Freund,  Jens
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95975

Wolber,  Vera
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93660

Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Freund, J., Kellner, R., Konvalinka, J., Wolber, V., Kräusslich, H.-G., & Kalbitzer, H. R. (1994). A possible regulation of negative factor (Nef) activity of human immunodeficiency virus type 1 by the viral protease. European Journal of Biochemistry, 223(2), 589-593. doi:10.1111/j.1432-1033.1994.tb19029.x.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-A8F8-F
Abstract
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.