Structure, Function, and Aggregation of the Zinc-Free Form of the p53 DNA Binding Domain†

Biochemistry ◽  
2003 ◽  
Vol 42 (8) ◽  
pp. 2396-2403 ◽  
Author(s):  
James S. Butler ◽  
Stewart N. Loh
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Binding Domain ◽  
Free Form ◽  
Dna Binding Domain

Structure, function, and dynamics of the dimerization and DNA-binding domain of oncogenic transcription factor v-Myc11Edited by P. E. Wright

2001 ◽  
Vol 307 (5) ◽  
pp. 1395-1410 ◽  
Author(s):  
Wolfgang Fieber ◽  
Martin L. Schneider ◽  
Theresia Matt ◽  
Bernhard Kräutler ◽  
Robert Konrat ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Structure Function ◽  
Binding Domain ◽  
Factor V ◽  
Dna Binding Domain ◽  
Oncogenic Transcription Factor

scholarly journals Rgg protein structure–function and inhibition by cyclic peptide compounds

2015 ◽  
Vol 112 (16) ◽  
pp. 5177-5182 ◽  
Author(s):  
Vijay Parashar ◽  
Chaitanya Aggarwal ◽  
Michael J. Federle ◽  
Matthew B. Neiditch
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Cyclosporin A ◽  
Crystal Structures ◽  
Disulfide Bond ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
X Ray ◽  
Peptide Pheromone ◽  
Dimerization Interface

Peptide pheromone cell–cell signaling (quorum sensing) regulates the expression of diverse developmental phenotypes (including virulence) in Firmicutes, which includes common human pathogens, e.g.,Streptococcus pyogenesandStreptococcus pneumoniae. Cytoplasmic transcription factors known as “Rgg proteins” are peptide pheromone receptors ubiquitous in Firmicutes. Here we present X-ray crystal structures of aStreptococcusRgg protein alone and in complex with a tight-binding signaling antagonist, the cyclic undecapeptide cyclosporin A. To our knowledge, these represent the first Rgg protein X-ray crystal structures. Based on the results of extensive structure–function analysis, we reveal the peptide pheromone-binding site and the mechanism by which cyclosporin A inhibits activation of the peptide pheromone receptor. Guided by the Rgg–cyclosporin A complex structure, we predicted that the nonimmunosuppressive cyclosporin A analog valspodar would inhibit Rgg activation. Indeed, we found that, like cyclosporin A, valspodar inhibits peptide pheromone activation of conserved Rgg proteins in medically relevantStreptococcusspecies. Finally, the crystal structures presented here revealed that the Rgg protein DNA-binding domains are covalently linked across their dimerization interface by a disulfide bond formed by a highly conserved cysteine. The DNA-binding domain dimerization interface observed in our structures is essentially identical to the interfaces previously described for other members of the XRE DNA-binding domain family, but the presence of an intermolecular disulfide bond buried in this interface appears to be unique. We hypothesize that this disulfide bond may, under the right conditions, affect Rgg monomer–dimer equilibrium, stabilize Rgg conformation, or serve as a redox-sensitive switch.

scholarly journals Structure-function analysis of the DNA binding domain ofSaccharomyces cerevisiaeABF1

1995 ◽  
Vol 23 (15) ◽  
pp. 2980-2987 ◽  
Author(s):  
Ginam Cho ◽  
Jiyoung Kim ◽  
Hyune Mo Rho ◽  
Guhung Jung
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Function Analysis ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals Structure-Function Studies of DNA Binding Domain of Response Regulator KdpE Reveals Equal Affinity Interactions at DNA Half-Sites

PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e30102 ◽  
Author(s):  
Anoop Narayanan ◽  
Lake N. Paul ◽  
Sakshi Tomar ◽  
Dipak N. Patil ◽  
Pravindra Kumar ◽  
...  
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Response Regulator ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals 2P054 The structure-function relationship between a novel DNA binding domain (STPR) and its tandem repeat unit

2005 ◽  
Vol 45 (supplement) ◽  
pp. S133
Author(s):  
D. Matsumoto ◽  
T. Yamaki ◽  
S. Saito ◽  
K. Kawaguchi ◽  
H. Yamamoto ◽  
...  
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Tandem Repeat ◽  
Repeat Unit ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Structure Function Relationship ◽  
Function Relationship

scholarly journals Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Andreas Schlundt ◽  
Sophie Buchner ◽  
Robert Janowski ◽  
Thomas Heydenreich ◽  
Ralf Heermann ◽  
...  
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Function Analysis ◽  
Transcriptional Activator ◽  
Binding Domain ◽  
Dna Binding Domain

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide
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