Molecular recognition of Fc-specific ligands binding onto the consensus binding site of IgG: insights from molecular simulation

2014 ◽  
Vol 27 (8) ◽  
pp. 501-509 ◽  
Author(s):  
Hong-Fei Tong ◽  
Dong-Qiang Lin ◽  
Qi-Lei Zhang ◽  
Rong-Zhu Wang ◽  
Shan-Jing Yao

1989 ◽  
Vol 9 (3) ◽  
pp. 1327-1331
Author(s):  
T M Fisch ◽  
R Prywes ◽  
R G Roeder

We have demonstrated that two sequence elements in the c-fos promoter can mediate the response of the gene to epidermal growth factor and the tumor promoter 12-O-tetradecanoyl phorbol-13-acetate (TPA). The first is the previously described serum response element. The second is a sequence element highly homologous to the consensus binding site for the HeLa cell transcription factor AP1. Although recent reports have shown that fos protein binds to AP1-binding sites through an interaction with AP1 protein and have raised the speculation that fos protein may negatively regulate expression of the c-fos gene via this interaction, we found no role for the AP1 consensus homology in the downregulation of c-fos expression following induction by epidermal growth factor and TPA.



2002 ◽  
Vol 22 (13) ◽  
pp. 4890-4901 ◽  
Author(s):  
Sophie Deltour ◽  
Sébastien Pinte ◽  
Cateline Guerardel ◽  
Bohdan Wasylyk ◽  
Dominique Leprince

ABSTRACT HIC1 (hypermethylated in cancer) and its close relative HRG22 (HIC1-related gene on chromosome 22) encode transcriptional repressors with five C2H2 zinc fingers and an N-terminal BTB/POZ autonomous transcriptional repression domain that is unable to recruit histone deacetylases (HDACs). Alignment of the HIC1 and HRG22 proteins from various species highlighted a perfectly conserved GLDLSKK/R motif highly related to the consensus CtBP interaction motif (PXDLSXK/R), except for the replacement of the virtually invariant proline by a glycine. HIC1 strongly interacts with mCtBP1 both in vivo and in vitro through this conserved GLDLSKK motif, thus extending the CtBP consensus binding site. The BTB/POZ domain does not interact with mCtBP1, but the dimerization of HIC1 through this domain is required for the interaction with mCtBP1. When tethered to DNA by fusion with the Gal4 DNA-binding domain, the HIC1 central region represses transcription through interactions with CtBP in a trichostatin A-sensitive manner. In conclusion, our results demonstrate that HIC1 mediates transcriptional repression by both HDAC-independent and HDAC-dependent mechanisms and show that CtBP is a HIC1 corepressor that is recruited via a variant binding site.



1998 ◽  
Vol 63 (16) ◽  
pp. 5430-5437 ◽  
Author(s):  
Da-Sheng Wang ◽  
Ao-Lin Hsu ◽  
Xueqin Song ◽  
Chi-Ming Chiou ◽  
Ching-Shih Chen


2004 ◽  
Vol 126 (10) ◽  
pp. 3185-3190 ◽  
Author(s):  
Michael Subat ◽  
Andrew S. Borovik ◽  
Burkhard König


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