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* Residue conservation analysis
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PDB id:
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Transcription/DNA
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Title:
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Crystal structure of the basic-helix-loop-helix domains of the heterodimer e47/neurod1 bound to DNA
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Structure:
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Transcription factor e2-alpha. Chain: a, c. Fragment: basic-helix-loop-helix domain. Engineered: yes. Neurogenic differentiation factor 1. Chain: b, d. Fragment: basic helix-loop-helix domain. Synonym: neurod1. Engineered: yes.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: tcf3. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: neurod1, neurod. Synthetic: yes. Other_details: synthesized oligonucleotide.
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Resolution:
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2.50Å
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R-factor:
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0.248
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R-free:
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0.289
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Authors:
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R.B.Rose,A.Longo,G.P.Guanga
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Key ref:
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A.Longo
et al.
(2008).
Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition.
Biochemistry,
47,
218-229.
PubMed id:
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Date:
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12-Jul-07
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Release date:
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04-Nov-08
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PROCHECK
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Headers
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References
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P15806
(TFE2_MOUSE) -
Transcription factor E2-alpha from Mus musculus
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Seq:
Struc:
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651 a.a.
56 a.a.*
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Biochemistry
47:218-229
(2008)
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PubMed id:
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Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition.
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A.Longo,
G.P.Guanga,
R.B.Rose.
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ABSTRACT
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The ubiquitous class I basic helix-loop-helix (bHLH) factor E47 forms
heterodimers with multiple tissue specific class II bHLH proteins to regulate
distinct differentiation pathways. In order to define how class I- class II
heterodimer partners are selected, we determined the crystal structure of the
E47-NeuroD1-bHLH dimer in complex with the insulin promoter E-box sequence.
Purification of the bHLH domain of E47-NeuroD1 indicates that E47 heterodimers
are stable in solution. The interactions between E47 and NeuroD1 in the
heterodimer are comparable to the interactions between E47 monomers in the
homodimer, including hydrogen bonding, buried hydrophobic surface, and packing
interactions. This is consistent with a model in which E47-NeuroD1 heterodimers
are favored due to the instability of NeuroD1 homodimers. Although E47-NeuroD1
is oriented uniquely on the E-box sequence (CATCTG) within the promoter of the
insulin gene, no direct contacts are observed with the central base pairs within
this E-box sequence. We propose that concerted domain motions allow E47 to form
specific base contacts in solution. NeuroD1 is restrained from adopting the same
base contacts by an additional phosphate backbone interaction by the
neurogenic-specific residue His115. Orienting E47-NeuroD1 on promoters may
foster protein-protein contacts essential to initiate transcription.
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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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V.P.Sharma,
A.L.Fenwick,
M.S.Brockop,
S.J.McGowan,
J.A.Goos,
A.J.Hoogeboom,
A.F.Brady,
N.O.Jeelani,
S.A.Lynch,
J.B.Mulliken,
D.J.Murray,
J.M.Phipps,
E.Sweeney,
S.E.Tomkins,
L.C.Wilson,
S.Bennett,
R.J.Cornall,
J.Broxholme,
A.Kanapin,
D.Johnson,
S.A.Wall,
P.J.van der Spek,
I.M.Mathijssen,
R.E.Maxson,
S.R.Twigg,
and
A.O.Wilkie
(2013).
Mutations in TCF12, encoding a basic helix-loop-helix partner of TWIST1, are a frequent cause of coronal craniosynostosis.
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Nat Genet,
45,
304-307.
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J.Richter,
M.Schlesner,
S.Hoffmann,
M.Kreuz,
E.Leich,
B.Burkhardt,
M.Rosolowski,
O.Ammerpohl,
R.Wagener,
S.H.Bernhart,
D.Lenze,
M.Szczepanowski,
M.Paulsen,
S.Lipinski,
R.B.Russell,
S.Adam-Klages,
G.Apic,
A.Claviez,
D.Hasenclever,
V.Hovestadt,
N.Hornig,
J.O.Korbel,
D.Kube,
D.Langenberger,
C.Lawerenz,
J.Lisfeld,
K.Meyer,
S.Picelli,
J.Pischimarov,
B.Radlwimmer,
T.Rausch,
M.Rohde,
M.Schilhabel,
R.Scholtysik,
R.Spang,
H.Trautmann,
T.Zenz,
A.Borkhardt,
H.G.Drexler,
P.Möller,
R.A.Macleod,
C.Pott,
S.Schreiber,
L.Trümper,
M.Loeffler,
P.F.Stadler,
P.Lichter,
R.Eils,
R.Küppers,
M.Hummel,
W.Klapper,
P.Rosenstiel,
A.Rosenwald,
B.Brors,
and
R.Siebert
(2012).
Recurrent mutation of the ID3 gene in Burkitt lymphoma identified by integrated genome, exome and transcriptome sequencing.
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Nat Genet,
44,
1316-1320.
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D.B.Sparrow,
D.Sillence,
M.A.Wouters,
P.D.Turnpenny,
and
S.L.Dunwoodie
(2010).
Two novel missense mutations in HAIRY-AND-ENHANCER-OF-SPLIT-7 in a family with spondylocostal dysostosis.
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Eur J Hum Genet,
18,
674-679.
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H.J.Yang,
A.O.Silva,
N.Koyano-Nakagawa,
and
S.C.McLoon
(2009).
Progenitor cell maturation in the developing vertebrate retina.
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Dev Dyn,
238,
2823-2836.
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D.B.Sparrow,
E.Guillén-Navarro,
D.Fatkin,
and
S.L.Dunwoodie
(2008).
Mutation of Hairy-and-Enhancer-of-Split-7 in humans causes spondylocostal dysostosis.
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Hum Mol Genet,
17,
3761-3766.
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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.
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Links
