 |
PDBsum entry 1paa
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transcription regulation
|
PDB id
|
|
|
|
1paa
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structure of a histidine-X4-Histidine zinc finger domain: insights into adr1-Uas1 protein-Dna recognition.
|
 |
|
Authors
|
 |
B.E.Bernstein,
R.C.Hoffman,
S.Horvath,
J.R.Herriott,
R.E.Klevit.
|
 |
|
Ref.
|
 |
Biochemistry, 1994,
33,
4460-4470.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The solution structure for a mutant zinc finger peptide based on the sequence of
the C-terminal ADR1 finger has been determined by two-dimensional NMR
spectroscopy. The mutant peptide, called PAPA, has both proline residues from
the wild-type sequence replaced with alanines. A nonessential cysteine was also
replaced with alanine. The behavior of PAPA in solution implicates the prolines
in the conformational heterogeneity reported earlier for the wild-type peptide
[Xu, R. X., Horvath, S. J., & Klevit, R. E. (1991) Biochemistry 30,
3365-3371]. The solution structure of PAPA reveals several interesting features
of the zinc finger motif. The residue immediately following the second cysteine
ligand adopts a positive phi angle, which we propose is a common feature of this
class of zinc fingers, regardless of whether this residue is a glycine. The NMR
spectrum and resulting solution structure of PAPA suggest that a side-chain to
side-chain hydrogen bond involving an arginine and an aspartic acid analogous to
one observed in the Zif268 protein-DNA cocrystal structure exists in solution in
the absence of DNA [Pavletich, N. P., & Pabo, C. O. (1991) Science 252,
809-817]. A model for the interaction between the two ADR1 zinc fingers and
their DNA binding sites was built by superpositioning the refined solution
structures of PAPA and ADR1b onto the Zif268 structure. This model offers
structural explanations for a variety of mutations to the ADR1 zinc finger
domains that have been shown to affect DNA-binding affinity or specificity.
|
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
A simple method for the refinement of models derived from nmr data demonstrated on a zinc-Finger domain from yeast adr1
|
 |
|
Authors
|
 |
R.C.Hoffman,
R.X.Xu,
R.E.Klevit,
J.R.Herriott.
|
 |
|
Ref.
|
 |
j magn reson ,ser b, 1993,
102,
61.
|
 |
 |
|
|
|
|
 |