Structure Comparison of Two Conserved HNF-3/fkh Proteins HFH-1 and Genesis Indicates the Existence of Folding Differences in Their Complexes with a DNA Binding Sequence

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• 作者：Wanyun Sheng ; Mark Rance ; and Xiubei Liao
• 刊名：Biochemistry
• 出版年：2002
• 出版时间：March 12, 2002
• 年：2002
• 卷：41
• 期：10
• 页码：3286 - 3293
• 全文大小：218K
• 年卷期：v.41,no.10(March 12, 2002)
• ISSN：1520-4995

文摘

The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a large number oftranscription factors that recognize divergent DNA sequences via a winged helix binding motif. HNF-3/fkh proteins show a broad profile of DNA sequence-specificity in which one DNA sequence can berecognized by more than one HNF-3/fkh protein and each individual HNF-3/fkh protein has several DNAbinding sequences. In this study, heteronuclear NMR methods were used to study the structures of theDNA binding domain of a conserved winged helix protein HFH-1 and its DNA complexes. The structuralcomparison of winged helix proteins HFH-1 and Genesis and their DNA complexes indicates that eventwo highly conserved HNF-3 family members can adopt different local structures when they contact anidentical DNA binding sequence, while one of these two HNF-3 proteins seems to adopt only slightlydifferent structures on different DNA binding sites.