2HFH

THE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES

Summary for 2HFH

• Entry DOI: 10.2210/pdb2hfh/pdb
• Descriptor: GENESIS (1 entity in total)
• Functional Keywords: hnf-3 homologues, winged helix protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus (By similarity): Q63245
• Total number of polymer chains: 1
• Total formula weight: 13049.02

Authors

Marsden, I.,Jin, C.,Liao, X. (deposition date: 1998-01-27, release date: 1998-06-17, Last modification date: 2024-05-29)

Primary citation

Marsden, I.,Jin, C.,Liao, X.
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.
J.Mol.Biol., 278:293-299, 1998

PubMed Abstract: 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.

PubMed: 9571051
DOI: 10.1006/jmbi.1998.1703

Experimental method

SOLUTION NMR