Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2004-8-2
pubmed:abstractText
Hepatocyte nuclear factor 6 (HNF-6) belongs to the family of One Cut transcription factors (also known as OC-1) and is essential for the development of the mouse pancreas, gall bladder, and the interhepatic bile ducts. HNF-6 binds to DNA as a monomer utilizing a single cut domain and a divergent homeodomain motif located at its C terminus. Here, we have used NMR methods to determine the solution structures of the 162 amino acid residue DNA-binding domain of the HNF-6alpha protein. The resulting overall structure of HNF-6alpha has two different distinct domains: the Cut domain and the Homeodomain connected by a long flexible linker. Our NMR structure shows that the Cut domain folds into a topology homologous to the POU DNA-binding domain, even though the sequences of these two protein families do not show homology. The DNA contact sequence of the HNF-6alpha was mapped with chemical shift perturbation methods. Our data also show that a proposed CREB-binding protein histone acetyltransferase protein-recruiting sequence, LSDLL, forms a helix and is involved in the hydrophobic core of the Cut domain. The structure implies that this sequence has to undergo structural changes when it interacts with CREB-binding protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response..., http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 1, http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 1-alpha, http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 6, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Hnf1a protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Octamer Transcription Factor-6, http://linkedlifedata.com/resource/pubmed/chemical/Onecut1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Pou3f1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Solutions, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33928-36
pubmed:dateRevised
2009-11-24
pubmed:meshHeading
pubmed-meshheading:15169783-Acetyltransferases, pubmed-meshheading:15169783-Amino Acid Sequence, pubmed-meshheading:15169783-Animals, pubmed-meshheading:15169783-Binding Sites, pubmed-meshheading:15169783-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:15169783-DNA, pubmed-meshheading:15169783-DNA-Binding Proteins, pubmed-meshheading:15169783-Hepatocyte Nuclear Factor 1, pubmed-meshheading:15169783-Hepatocyte Nuclear Factor 1-alpha, pubmed-meshheading:15169783-Hepatocyte Nuclear Factor 6, pubmed-meshheading:15169783-Histone Acetyltransferases, pubmed-meshheading:15169783-Homeodomain Proteins, pubmed-meshheading:15169783-Magnetic Resonance Spectroscopy, pubmed-meshheading:15169783-Mice, pubmed-meshheading:15169783-Models, Molecular, pubmed-meshheading:15169783-Molecular Sequence Data, pubmed-meshheading:15169783-Molecular Structure, pubmed-meshheading:15169783-Nuclear Proteins, pubmed-meshheading:15169783-Octamer Transcription Factor-6, pubmed-meshheading:15169783-Protein Folding, pubmed-meshheading:15169783-Sequence Homology, pubmed-meshheading:15169783-Solutions, pubmed-meshheading:15169783-Trans-Activators, pubmed-meshheading:15169783-Transcription Factors
pubmed:year
2004
pubmed:articleTitle
Structure of the hepatocyte nuclear factor 6alpha and its interaction with DNA.
pubmed:affiliation
Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60607, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't