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

Two-dimensional1H-nmr studies on thelac repressor DNA binding domain: Further resonance assignments and identification of nuclear overhauser enhancements

Biopolymers ◽  
1985 ◽  
Vol 24 (12) ◽  
pp. 2257-2277 ◽  
Author(s):  
E. R. P. Zuiderweg ◽  
R. M. Scheek ◽  
R. Kaptein
Keyword(s):  
Dna Binding ◽  
Resonance Assignments ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies ◽  
Nuclear Overhauser

NMR studies of the POU-specific DNA-binding domain of Oct-1: Sequential proton and nitrogen-15 assignments and secondary structure

Biochemistry ◽  
1993 ◽  
Vol 32 (23) ◽  
pp. 6032-6040 ◽  
Author(s):  
Michel Cox ◽  
Niek Dekker ◽  
Rolf Boelens ◽  
C. Peter Verrijzer ◽  
Peter C. van der Vliet ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies

NMR Studies of the Human Retinoic Acid Receptor-? DNA-Binding Domain.

1993 ◽  
Vol 684 (1 Zinc-Finger P) ◽  
pp. 49-62 ◽  
Author(s):  
R. M. A. KNEGTEL ◽  
R. BOELENS ◽  
M. L. GANADU ◽  
A. V. E. GEORGE ◽  
M. KATAHIRA ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Dna Binding ◽  
Retinoic Acid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies ◽  
Acid Receptor

Proton NMR studies of the glucocorticoid receptor DNA-binding domain: sequential assignments and identification of secondary structure elements

Biochemistry ◽  
1990 ◽  
Vol 29 (38) ◽  
pp. 9015-9023 ◽  
Author(s):  
T. Haerd ◽  
E. Kellenbach ◽  
R. Boelens ◽  
K. Dahlman ◽  
J. Carlstedt-Duke ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Proton Nmr ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies

Heteronuclear Strategies for the Assignment of Larger protein/DNA complexes: Application to the 37 kDa trp Represser-Operator Complex

1997 ◽  
Author(s):  
M.J. Revington ◽  
W. Lee
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies ◽  
Dna Complexes ◽  
Dna Binding Domains ◽  
Binding Domains

The sequence-specific DNA binding function of many proteins is recognized as one of the central mechanisms of regulating transcription and DNA replication and repair. The ability of these proteins to select a short (usually 10 to 20 basepair) sequence out of the entire genome with which to form a stable complex is a prime example of molecular recognition. Atomic resolution structural studies using NMR and X-ray crystallography have emerged as essential techniques in understanding the basis of specificity and stability in these systems. While NMR studies of small DNA-binding domains of proteins have become almost routine (see Kaptein, 1993 for a review) relatively few NMR studies of protein-DNA complexes have been reported. These include the lac repressor headpiece complex (Chuprina et al., 1993). the Antennapedia homeodomain complex (Billetere et al., 1993), the GATA-1 complex (Omichinski et al., 1993). and the Myb DNA binding domain complex (Ogata et al., 1993); all of these complexes are smaller than 20 kDa. In most cases, size limitations have meant that only the DNA binding domain of the protein in complex with a single binding element have been studied. In vivo, however, most DNA binding proteins are much larger than these domains and often function as oligomers. The decrease in quality and increase in complexity of spectra as the molecular weight of the sample increases, limits the number of systems amenable to study using NMR and influences the decision to focus on single domains of multidomain proteins. However, since many DNA-binding proteins are regulated by the binding of ligands, other proteins or phosphorylation, often at sites distal from the DNA-binding domain, it is preferable to study as much of the intact protein as possible in order to characterize allosteric and regulatory mechanisms (Pabo and Sauer, 1992). E. coli trp repressor is a 25 kDa homodimer that regulates operons involved in tryptophan biosynthesis. The dimer is one of the smallest intact proteins that binds sequence specifically to DNA and whose affinity is modulated by an effector (L-tryptophan).

Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor

Biochemistry ◽  
1990 ◽  
Vol 29 (39) ◽  
pp. 9218-9225 ◽  
Author(s):  
Tao Pan ◽  
Leonard P. Freedman ◽  
Joseph E. Coleman
Keyword(s):  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Nmr Studies

scholarly journals Primary structure of a glycosylated DNA-binding domain in human plasma fibronectin.

1985 ◽  
Vol 260 (4) ◽  
pp. 2301-2306
Author(s):  
H Pande ◽  
J Calaycay ◽  
D Hawke ◽  
C M Ben-Avram ◽  
J E Shively
Keyword(s):  
Dna Binding ◽  
Human Plasma ◽  
Primary Structure ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Plasma Fibronectin
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