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PDBsum entry 4aa6
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Transcription/DNA
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PDB id
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4aa6
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Contents |
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69 a.a.
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70 a.a.
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68 a.a.
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69 a.a.
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PDB id:
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Transcription/DNA
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Title:
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The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
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Structure:
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Estrogen receptor. Chain: a, b, e, f. Fragment: residues 182-252. Synonym: er, er-alpha, estradiol receptor, nuclear receptor subfamily 3 group a member 1. Engineered: yes. 5'-d( Cp Tp Ap Ap Gp Tp Cp Ap Cp Ap Gp Tp Gp Ap Cp Cp Tp G)-3'. Chain: c, g.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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Authors:
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J.W.Schwabe,L.Chapman,D.Rhodes
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Key ref:
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J.W.Schwabe
et al.
(1995).
The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation.
Structure,
3,
201-213.
PubMed id:
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Date:
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30-Nov-11
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Release date:
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14-Dec-11
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PROCHECK
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Headers
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References
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P03372
(ESR1_HUMAN) -
Estrogen receptor from Homo sapiens
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Seq:
Struc:
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595 a.a.
69 a.a.
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P03372
(ESR1_HUMAN) -
Estrogen receptor from Homo sapiens
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Seq:
Struc:
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595 a.a.
70 a.a.
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Enzyme class:
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Chains A, B, E, F:
E.C.?
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Structure
3:201-213
(1995)
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PubMed id:
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The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation.
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J.W.Schwabe,
L.Chapman,
D.Rhodes.
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ABSTRACT
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BACKGROUND: Structural studies of protein-DNA complexes have tended to give the
impression that DNA recognition requires a unique molecular interface. However,
many proteins recognize DNA targets that differ from what is thought to be their
ideal target sequence. The steroid hormone receptors illustrate this problem in
recognition rather well, since consensus DNA targets are rare. RESULTS: Here we
describe the structure, at 2.6 A resolution, of a complex between a dimer of the
DNA-binding domain from the human oestrogen receptor (ERDBD) and a non-consensus
DNA target site in which there is a single base substitution in one half of the
palindromic binding site. This substitution results in a 10-fold increase in the
dissociation constant of the ERDBD-DNA complex. Comparison of this structure
with a structure containing a consensus DNA-binding site determined previously,
shows that recognition of the non-consensus sequence is achieved by the
rearrangement of a lysine side chain so as to make an alternative base contact.
CONCLUSIONS: This study suggests that proteins adapt to recognize different DNA
sequences by rearranging side chains at the protein-DNA interface so as to form
alternative patterns of intermolecular contacts.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.L.Nott,
Y.Huang,
X.Li,
B.R.Fluharty,
X.Qiu,
W.V.Welshons,
S.Yeh,
and
M.Muyan
(2009).
Genomic responses from the estrogen-responsive element-dependent signaling pathway mediated by estrogen receptor alpha are required to elicit cellular alterations.
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J Biol Chem,
284,
15277-15288.
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C.G.Kalodimos,
A.M.Bonvin,
R.K.Salinas,
R.Wechselberger,
R.Boelens,
and
R.Kaptein
(2002).
Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain.
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EMBO J,
21,
2866-2876.
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PDB code:
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P.J.van Tilborg,
M.Czisch,
F.A.Mulder,
G.E.Folkers,
A.M.Bonvin,
M.Nair,
R.Boelens,
and
R.Kaptein
(2000).
Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site.
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Biochemistry,
39,
8747-8757.
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P.J.van Tilborg,
F.A.Mulder,
M.M.de Backer,
M.Nair,
E.C.van Heerde,
G.Folkers,
P.T.van der Saag,
Y.Karimi-Nejad,
R.Boelens,
and
R.Kaptein
(1999).
Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation.
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Biochemistry,
38,
1951-1956.
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S.Chusacultanachai,
K.A.Glenn,
A.O.Rodriguez,
E.K.Read,
J.F.Gardner,
B.S.Katzenellenbogen,
and
D.J.Shapiro
(1999).
Analysis of estrogen response element binding by genetically selected steroid receptor DNA binding domain mutants exhibiting altered specificity and enhanced affinity.
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J Biol Chem,
274,
23591-23598.
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N.C.Horton,
and
J.J.Perona
(1998).
Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts.
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J Biol Chem,
273,
21721-21729.
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PDB code:
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H.Berglund,
M.Wolf-Watz,
T.Lundbäck,
S.van den Berg,
and
T.Härd
(1997).
Structure and dynamics of the glucocorticoid receptor DNA-binding domain: comparison of wild type and a mutant with altered specificity.
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Biochemistry,
36,
11188-11197.
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R.Solano,
A.Fuertes,
L.Sánchez-Pulido,
A.Valencia,
and
J.Paz-Ares
(1997).
A single residue substitution causes a switch from the dual DNA binding specificity of plant transcription factor MYB.Ph3 to the animal c-MYB specificity.
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J Biol Chem,
272,
2889-2895.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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