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PDBsum entry 3m9e
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Transcription/DNA
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PDB id
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3m9e
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Transcription/DNA
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Title:
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Thyroid hormone beta DNA binding domain homodimer with inverted palindrome tre
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Structure:
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Thyroid hormone receptor beta. Chain: a, b, e, f. Fragment: DNA binding domain (unp residues 104 to 206). Synonym: c-erba-beta, c-erba-2, nuclear receptor subfamily 1 group a member 2. Engineered: yes. DNA (5'- d( Ap Tp Tp Gp Ap Cp Cp Tp Cp Ap Gp Cp Tp Gp Ap Gp Gp Tp Cp Ap Ap T)- 3').
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: erba2, nr1a2, rod, thrb. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the sequence is idealized
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Resolution:
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2.41Å
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R-factor:
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0.182
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R-free:
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0.231
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Authors:
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Y.Chen
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Key ref:
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Y.Chen
and
M.A.Young
(2010).
Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element.
Mol Endocrinol,
24,
1650-1664.
PubMed id:
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Date:
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22-Mar-10
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Release date:
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18-Aug-10
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PROCHECK
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Headers
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References
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P18113
(THB_RAT) -
Thyroid hormone receptor beta from Rattus norvegicus
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Seq:
Struc:
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461 a.a.
101 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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A-T-T-G-A-C-C-T-C-A-G-C-T-G-A-G-G-T-C-A-A-T
22 bases
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A-T-T-G-A-C-C-T-C-A-G-C-T-G-A-G-G-T-C-A-A-T
22 bases
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A-T-T-G-A-C-C-T-C-A-G-C-T-G-A-G-G-T-C-A-A-T
22 bases
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A-T-T-G-A-C-C-T-C-A-G-C-T-G-A-G-G-T-C-A-A-T
22 bases
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Mol Endocrinol
24:1650-1664
(2010)
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PubMed id:
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Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element.
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Y.Chen,
M.A.Young.
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ABSTRACT
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Thyroid hormone receptor (TR), as a member of the nuclear hormone receptor
family, can recognize and bind different classes of DNA response element targets
as either a monomer, a homooligomer, or a heterooligomer. We report here the
first crystal structure of a homodimer TR DNA-binding domain (DBD) in complex
with an inverted repeat class of thyroid response element (TRE). The structure
shows a nearly symmetric structure of the TR DBD assembled on the F2 TRE where
the base recognition contacts in the homodimer DNA complex are conserved
relative to the previously published structure of a TR-9-cis-retinoic acid
receptor heterodimer DNA complex. The new structure also reveals that the T-box
region of the DBD can function as a structural hinge that enables a large degree
of flexibility in the position of the C-terminal extension helix that connects
the DBD to the ligand-binding domain. Although the isolated TR DBDs exist as
monomers in solution, we have measured highly cooperative binding of the two TR
DBD subunits onto the inverted repeat DNA sequence. This suggests that elements
of the DBD can influence the specific TR oligomerization at target genes, and it
is not just interactions between the ligand-binding domains that are responsible
for TR oligomerization at target genes. Mutational analysis shows that
intersubunit contacts at the DBD C terminus account for some, but not all, of
the cooperative homodimer TR binding to the inverted repeat class TRE.
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Links
