Effect of Zn2+on DNA Recognition and Stability of the p53 DNA-Binding Domain†

Biochemistry ◽  
2006 ◽  
Vol 45 (24) ◽  
pp. 7483-7492 ◽  
Author(s):  
Jianxin Duan ◽  
Lennart Nilsson
Keyword(s):  
Dna Binding ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain

The cavity in the hydrophobic core of Myb DNA-binding domain is reserved for DNA recognition and trans-activation

1996 ◽  
Vol 3 (2) ◽  
pp. 178-187 ◽  
Author(s):  
Kazuhiro Ogata ◽  
Chie Kanei-Ishii ◽  
Motoko Sasaki ◽  
Hideki Hatanaka ◽  
Aritaka Nagadoi ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Hydrophobic Core

DNA recognition by nuclear receptors

2004 ◽  
Vol 40 ◽  
pp. 59-72 ◽  
Author(s):  
Frank Claessens ◽  
Daniel T Gewirth
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Nuclear Receptors ◽  
Dna Sequences ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Core Motif ◽  
Response Elements ◽  
Sequence Recognition

The nuclear receptors constitute a large family of ligand-inducible transcription factors. The control of many genetic pathways requires the assembly of these nuclear receptors in defined transcription-activating complexes within control regions of ligand-responsive genes. An essential step is the interaction of the receptors with specific DNA sequences, called hormone-response elements (HREs). These response elements position the receptors, and the complexes recruited by them, close to the genes of which transcription is affected. HREs are bipartite elements that are composed of two hexameric core half-site motifs. The identity of the response elements resides in three features: the nucleotide sequence of the two core motif half-sites, the number of base pairs separating them and the relative orientation of the motifs. The DNA-binding domains of nuclear receptors consist of two zinc-nucleated modules and a C-terminal extension. Residues in the first module determine the specificity of the DNA recognition, while residues in the second module are involved in dimerization. Indeed, nuclear receptors bind to their HREs as either homodimers or heterodimers. Depending on the type of receptor, the C-terminal extension plays a role in sequence recognition, dimerization, or both. The DNA-binding domain is furthermore involved in several other functions including nuclear localization, and interaction with transcription factors and co-activators. It is also the target of post-translational modifications. The DNA-binding domain therefore plays a central role, not only in the correct binding of the receptors to the target genes, but also in the control of other steps of the action mechanism of nuclear receptors.

Myb−DNA Recognition:  Role of Tryptophan Residues and Structural Changes of the Minimal DNA Binding Domain of c-Myb

Biochemistry ◽  
1999 ◽  
Vol 38 (6) ◽  
pp. 1921-1929 ◽  
Author(s):  
Loussinée Zargarian ◽  
Véronique Le Tilly ◽  
Nadège Jamin ◽  
Alain Chaffotte ◽  
Odd S. Gabrielsen ◽  
...  
Keyword(s):  
Dna Binding ◽  
Structural Changes ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Tryptophan Residues

Response regulator YycF essential for bacterial growth: X-ray crystal structure of the DNA-binding domain and its PhoB-like DNA recognition motif

FEBS Letters ◽  
2008 ◽  
Vol 582 (23-24) ◽  
pp. 3434-3438 ◽  
Author(s):  
Toshihide Okajima ◽  
Akihiro Doi ◽  
Ario Okada ◽  
Yasuhiro Gotoh ◽  
Katsuyuki Tanizawa ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Bacterial Growth ◽  
Response Regulator ◽  
Dna Recognition ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
X Ray ◽  
Recognition Motif
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