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PDBsum entry 1ocp
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DNA binding protein
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PDB id
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1ocp
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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 the oct-3 pou-Homeodomain in solution, As determined by triple resonance heteronuclear multidimensional nmr spectroscopy.
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Authors
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E.H.Morita,
M.Shirakawa,
F.Hayashi,
M.Imagawa,
Y.Kyogoku.
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Ref.
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Protein Sci, 1995,
4,
729-739.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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The POU-homeodomain (POUH) forms the bipartite DNA-binding POU domain in
association with the POU-specific domain. The 1H, 15N, and 13C magnetic
resonances of the 67-amino acid long POUH of mouse Oct-3 have almost completely
been assigned, mainly through the combined use of three-dimensional triple
resonance NMR methods. Based on the distance and dihedral angle constraints
derived from the NMR data, the solution structure of the POUH domain has been
calculated by the ab initio simulated annealing method. The average RMS
deviation for all backbone heavy atoms of the 20 best calculated structures for
residues 9-53 of the total 67 amino acid residues is 0.44 A. The POUH domain
consists of three alpha-helices (helix-I, 10-20; helix-II, 28-38; and helix-III,
42-53), and helices-II and -III form a helix-turn-helix motif. In comparison
with other classical homeodomains, the folding of the three helices is quite
similar. However, the length of helix-III is fairly short. In the complex of the
Oct-1 POU domain with an octamer site (Klemm JD, et al., 1994, Cell 77:21-32),
the corresponding region is involved in helix-III. The structural difference
between these two cases will be discussed.
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Secondary reference #1
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Title
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Secondary structure of the oct-3 pou homeodomain as determined by 1h-15n nmr spectroscopy.
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Authors
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E.H.Morita,
M.Shirakawa,
F.Hayashi,
M.Imagawa,
Y.Kyogoku.
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Ref.
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FEBS Lett, 1993,
321,
107-110.
[DOI no: ]
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PubMed id
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