2hfh
From Proteopedia
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THE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES
Overview
The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a, large number of transcription factors and folds into a winged helix motif., Despite having almost invariable amino acid sequences in their principal, DNA-binding helices, HNF-3/fkh proteins show a wide diversity of, sequence-specific binding. Previous studies of chimeric HNF-3/fkh proteins, demonstrated that the binding specificity is primarily influenced by a, region directly adjacent to the binding helix. We report our findings of, an NMR structural study performed on an HNF-3/fkh family member (Genesis, formerly HFH-2) and compare it to that of another family member, (HNF-3gamma) complexed to DNA and determined by X-ray crystallography. It, is found that in comparison to HNF-3gamma, Genesis contains an extra small, helix directly prior to the N terminus of the primary DNA contact helix., Due to the insertion of this helix, a shorter and slightly re-positioned, primary DNA contact helix is observed, which we believe leads to the, DNA-binding specificity differences among family members.
About this Structure
2HFH is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural changes in the region directly adjacent to the DNA-binding helix highlight a possible mechanism to explain the observed changes in the sequence-specific binding of winged helix proteins., Marsden I, Jin C, Liao X, J Mol Biol. 1998 May 1;278(2):293-9. PMID:9571051
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