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PDBsum entry 1va2
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Transcription
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PDB id
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1va2
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References listed in PDB file
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Key reference
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Title
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Nmr structure of transcription factor sp1 DNA binding domain.
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Authors
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S.Oka,
Y.Shiraishi,
T.Yoshida,
T.Ohkubo,
Y.Sugiura,
Y.Kobayashi.
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Ref.
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Biochemistry, 2004,
43,
16027-16035.
[DOI no: ]
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PubMed id
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Abstract
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To understand the DNA recognition mechanism of zinc finger motifs of
transcription factor Sp1, we have determined the solution structure of
DNA-binding domain of the Sp1 by solution NMR techniques. The DNA-binding domain
of Sp1 consists of three Cys(2)His(2)-type zinc finger motifs. They have typical
betabetaalpha zinc finger folds and relatively random orientations. From
DNA-binding analysis performed by NMR and comparison between structures
determined here and previously reported structures of other zinc fingers, it was
assumed that DNA recognition modes of fingers 2 and 3 would be similar to those
of fingers of Zif268, in which each finger recognizes four base pairs strictly
by using residues at positions -1, 2, 3, and 6 of the recognition helix. On the
contrary, finger 1 can use only two residues for DNA recognition, Lys550 and
His553 at positions -1 and 3 of the helix, and has more relaxed sequence and
site specificity than other Cys(2)His(2) zinc fingers. It is proposed that this
relaxed property of finger 1 allows transcription factor Sp1 to bind various DNA
sequences with high affinity.
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