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PDBsum entry 1au7
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Transcription/DNA
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PDB id
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1au7
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of pit-1 pou domain bound to DNA as a dimer: unexpected arrangement and flexibility.
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Authors
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E.M.Jacobson,
P.Li,
A.Leon-Del-Rio,
M.G.Rosenfeld,
A.K.Aggarwal.
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Ref.
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Genes Dev, 1997,
11,
198-212.
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PubMed id
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Abstract
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Pit-1, a member of the POU domain family of transcription factors, characterized
by a bipartite DNA-binding domain, serves critical developmental functions based
on binding to diverse DNA elements in its target genes. Here we report a high
resolution X-ray analysis of the Pit-1 POU domain bound to a DNA element as a
homodimer. This analysis reveals that Pit-1 subdomains bind to perpendicular
faces of the DNA, rather than opposite faces of the DNA as in Oct-1. This is
accomplished by different spacing and orientation of the POU-specific domain.
Contrary to previous predictions, the dimerization interface involves the
carboxyl terminus of the DNA recognition helix of the homeodomain, which in an
extended conformation interacts with specific residues at the amino terminus of
helix alpha1 and in the loop between helices alpha3 and alpha4 of the
POU-specific domain of the symmetry related monomer. These features suggest the
molecular basis of disease-causing mutations in Pit-1 and provide potential
basis for the flexible allostery between protein domains and DNA sites in the
activation of target genes.
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