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NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1.
The three-dimensional solution structure of a complex between the DNA binding domain of the chicken erythroid transcription factor GATA-1 and its cognate DNA site has been determined withExpand
Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53.
The structure reveals that p53 forms a nine residue amphipathic alpha helix upon binding to Tfb1, and it is demonstrated that diphosphorylation of p53 at Ser46 and Thr55 leads to a significant enhancement in p53 binding to p62 and TFB1. Expand
Use of dipolar 1H–15N and 1H–13C couplings in the structure determination of magnetically oriented macromolecules in solution
The resulting residual dipolar couplings contain information on the orientation of the internuclear vectors relative to the molecular magnetic susceptibility tensor, thereby providing information on long range order that is not accessible by any of the solution NMR parameters currently used in structure determination. Expand
The single Cys2-His2 zinc finger domain of the GAGA protein flanked by basic residues is sufficient for high-affinity specific DNA binding.
Using a series of deletion mutants, it was demonstrated that the minimal domain required for specific binding includes a single zinc finger of the Cys2-His2 family and a stretch of basic amino acids located on the N-terminal end of the zinc finger. Expand
Purple membrane induced alignment of biological macromolecules in the magnetic field
The general possibility to align biological macromolecules in the magnetic field by the presence of orienting agents such as lipid bicelles has led to a wealth of new structural parameters which canExpand
A palindromic regulatory site within vertebrate GATA-1 promoters requires both zinc fingers of the GATA-1 DNA-binding domain for high-affinity interaction
It is proposed that GATApal, a palindromic site composed of one complete [(A/T)GATA(A/G)] and one partial (GAT) canonical motif, is important for positive regulation of GATA-1 expression in erythroid cells. Expand
The solution structure of a specific GAGA factor–DNA complex reveals a modular binding mode
The structure of a complex between the DMA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magneticExpand
A Motif Shared by TFIIF and TFIIB Mediates Their Interaction with the RNA Polymerase II Carboxy-Terminal Domain Phosphatase Fcp1p in Saccharomyces cerevisiae
Results suggest strongly that this KEFGK motif in RAP74 mediates its interaction with Fcp1p in vivo, and is important for cell viability, mRNA synthesis, and CTD dephosphorylation in vivo. Expand
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
The three-dimensional structure of the oligomerization domain of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy and the tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. Expand
Structural and functional evidence that Rad4 competes with Rad2 for binding to the Tfb1 subunit of TFIIH in NER
It is shown that Rad4 binds the PH domain of the Tfb1 (Tfb1PH) with high affinity, which supports the hypothesis that XPG/Rad2 displaces XPC/Rad4 from the repair complex in part through interactions with the TFB1/p62 subunit of TFIIH. Expand