2d5v
From Proteopedia
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Crystal structure of HNF-6alpha DNA-binding domain in complex with the TTR promoter
Overview
Hepatocyte nuclear factor-6 (HNF-6), a liver-enriched transcription, factor, controls the development of various tissues, such as the pancreas, and liver, and regulates the expression of several hepatic genes. This, protein belongs to the ONECUT class of homeodomain proteins and contains a, bipartite DNA-binding domain composed of a single cut domain and a, characteristic homeodomain. This transcription factor has two distinct, modes of DNA binding and transcriptional activation that use different, coactivators depending on the target gene. The crystal structure of the, bipartite DNA-binding domain of HNF-6alpha complexed with the, HNF-6-binding site of the TTR promoter revealed the DNA recognition, mechanism of this protein. Comparing our structure with the DNA-free, structure of HNF-6 or the structure of Oct-1, we discuss characteristic, features associated with DNA binding and the structural basis for the dual, mode of action of this protein, and we suggest a strategy for variability, of transcriptional activation of the target gene.
About this Structure
2D5V is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
Reference
DNA recognition mechanism of the ONECUT homeodomain of transcription factor HNF-6., Iyaguchi D, Yao M, Watanabe N, Nishihira J, Tanaka I, Structure. 2007 Jan;15(1):75-83. PMID:17223534
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