scholarly journals Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif

Virology ◽  
2006 ◽  
Vol 349 (2) ◽  
pp. 290-299 ◽  
Author(s):  
Zuoxiang Xiao ◽  
Elana Ehrlich ◽  
Yunkai Yu ◽  
Kun Luo ◽  
Tao Wang ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Binding Domain ◽  
Zinc Binding ◽  
Zinc Binding Domain ◽  
Hiv 1 ◽  
Hydrophobic Interface

scholarly journals Solution structure of the His 12 → Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium

1998 ◽  
Vol 7 (12) ◽  
pp. 2669-2674 ◽  
Author(s):  
Mengli Cai ◽  
Michael Caffrey ◽  
G. Marius Clore ◽  
Angela M. Gronenborn ◽  
Ying Huang ◽  
...  
Keyword(s):  
Solution Structure ◽  
Binding Domain ◽  
Zinc Binding ◽  
Zinc Binding Domain ◽  
Hiv 1

Solution structure of the N-terminal zinc binding domain of HIV-1 integrase

1997 ◽  
Vol 4 (7) ◽  
pp. 567-577 ◽  
Author(s):  
Mengli Cai ◽  
Ronglan Zheng ◽  
Michael Caffrey ◽  
Robert Craigie ◽  
G. Marius Clore ◽  
...  
Keyword(s):  
Solution Structure ◽  
Binding Domain ◽  
Zinc Binding ◽  
Zinc Binding Domain ◽  
Hiv 1

scholarly journals Subcellular Localization of Feline Immunodeficiency Virus Integrase and Mapping of Its Karyophilic Determinant

2003 ◽  
Vol 77 (8) ◽  
pp. 4516-4527 ◽  
Author(s):  
Cora L. Woodward ◽  
Yao Wang ◽  
Wendy J. Dixon ◽  
Han Htun ◽  
Samson A. Chow
Keyword(s):  
Subcellular Localization ◽  
Nuclear Import ◽  
Feline Immunodeficiency Virus ◽  
Fluorescent Protein ◽  
Basic Amino Acid ◽  
Binding Domain ◽  
Zinc Binding ◽  
Immunodeficiency Virus ◽  
Zinc Binding Domain ◽  
Hiv 1

ABSTRACT Feline immunodeficiency virus (FIV), like other members of the lentivirus subfamily, such as human immunodeficiency virus type 1 (HIV-1), can infect nondividing and terminally differentiated cells. The transport of the preintegration complex into the nucleus is cell cycle-independent, but the mechanism is not well understood. Integrase is a key component of the complex and has been suggested to play a role in nuclear import during HIV-1 replication. To determine its karyophilic property, FIV integrase fused with glutathione S-transferase and enhanced green fluorescent protein was expressed in various feline and human cells and the subcellular localization was visualized by fluorescence microscopy. Wild-type FIV integrase was karyophilic in all cell lines tested and capable of targeting the fusion protein to the nuclei of transfected cells. Analysis of deletion and point mutation variants of FIV integrase failed to reveal any canonical nuclear localization signal, and the karyophilic determinant was mapped to the highly conserved N-terminal zinc-binding HHCC motif. A region near the C-terminal domain enriched with basic amino acid residues also affected the nuclear import of integrase. However, the role of this region is only modulatory in comparison to that of the zinc-binding domain. The N-terminal zinc-binding domain does not bind DNA and instead is essential in integrase multimerization. We therefore postulate that the karyophilic property of FIV integrase requires subunit multimerization promoted by the HHCC motif. Alternatively, the HHCC motif may directly promote interaction between FIV integrase and cellular proteins involved in nuclear import.

scholarly journals Insight into the Roles of the 140-149 Catalytic Loop and the Zinc-Binding Domain for HIV-1 Integrase Activity

2009 ◽  
Vol 96 (3) ◽  
pp. 62a
Author(s):  
Kevin Carayon ◽  
Li Na ◽  
Olivier Delelis ◽  
Francoise Simon ◽  
Jean-Francois Mouscadet ◽  
...  
Keyword(s):  
Binding Domain ◽  
Zinc Binding ◽  
Catalytic Loop ◽  
Zinc Binding Domain ◽  
Insight Into ◽  
Hiv 1

EXAFS analysis of the zinc-binding domain of boar spermatidal transition protein 2

2001 ◽  
Vol 8 (2) ◽  
pp. 993-995
Author(s):  
Takeshi Kawai ◽  
Takehisa Konishi ◽  
Takashi Fujikawa ◽  
Atushi Sekine ◽  
Lica F. Imai ◽  
...  
Keyword(s):  
Binding Domain ◽  
Zinc Binding ◽  
Exafs Analysis ◽  
Zinc Binding Domain ◽  
Transition Protein

scholarly journals Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development.

1995 ◽  
Vol 14 (23) ◽  
pp. 5947-5956 ◽  
Author(s):  
K. L. Borden ◽  
J. M. Lally ◽  
S. R. Martin ◽  
N. J. O'Reilly ◽  
L. D. Etkin ◽  
...  
Keyword(s):  
Binding Domain ◽  
Zinc Binding ◽  
Xenopus Development ◽  
Zinc Binding Domain
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