Format

Send to

Choose Destination
Mol Cells. 1999 Jun 30;9(3):281-5.

The cytoplasmic domain of HIV-1 gp41 interacts with the carboxyl-terminal region of alpha-catenin.

Author information

1
Division of Life Science, College of National Sciences, Pai Chai University, Taejon, Korea.

Abstract

To know the cellular protein interactions with the viral protein can give an insight into the molecular mechanisms of the virus life cycle. As the function of the cytoplasmic domain of human immunodeficiency virus type 1 (HIV-1) gp41 is not known clearly, we searched for a cellular protein that interacts with the cytoplasmic domain of the HIV-1 gp41 using the yeast two-hybrid assay system. Screening of HeLa cell cDNA library yielded alpha-catenin cDNA. The cytoplasmic domain of the HIV-1 gp41 and the simian immunodeficiency virus (SIV) gp41 were able to interact with the carboxyl-terminal region of alpha-catenin specifically. Mapping of the interaction sites revealed that the interaction between the domain containing the second helix structure from the carboxyl-terminus of HIV-1 gp41 and the carboxyl-terminal region of alpha-catenin was stronger than other domains of gp41.

PMID:
10420987
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Publishing M2Community
Loading ...
Support Center