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2H8R

Hepatocyte Nuclear Factor 1b bound to DNA: MODY5 Gene Product

Summary for 2H8R
Entry DOI10.2210/pdb2h8r/pdb
Descriptor5'-D(*CP*TP*TP*GP*GP*TP*TP*AP*AP*TP*AP*AP*TP*TP*CP*AP*CP*CP*AP*G)-3', 5'-D(*GP*CP*TP*GP*GP*TP*GP*AP*AP*TP*TP*AP*TP*TP*AP*AP*CP*CP*AP*A)-3', Hepatocyte nuclear factor 1-beta, ... (4 entities in total)
Functional Keywordstrasncription factor, pou, homeo, protein-dna, human disease, transcription activator-dna complex, transcription activator/dna
Biological sourceHomo sapiens (human)
Cellular locationNucleus: P35680
Total number of polymer chains4
Total formula weight63688.69
Authors
Lu, P.,Rha, G.B.,Chi, Y.I. (deposition date: 2006-06-07, release date: 2007-06-19, Last modification date: 2023-08-30)
Primary citationLu, P.,Rha, G.B.,Chi, Y.I.
Structural basis of disease-causing mutations in hepatocyte nuclear factor 1beta.
Biochemistry, 46:12071-12080, 2007
Cited by
PubMed Abstract: HNF1beta is an atypical POU transcription factor that participates in a hierarchical network of transcription factors controlling the development and proper function of vital organs such as liver, pancreas, and kidney. Many inheritable mutations on HNF1beta are the monogenic causes of diabetes and several kidney diseases. To elucidate the molecular mechanism of its function and the structural basis of mutations, we have determined the crystal structure of human HNF1beta DNA binding domain in complex with a high-affinity promoter. Disease-causing mutations have been mapped to our structure, and their predicted effects have been tested by a set of biochemical/ functional studies. These findings together with earlier findings with a homologous protein HNF1alpha, help us to understand the structural basis of promoter recognition by these atypical POU transcription factors and the site-specific functional disruption by disease-causing mutations.
PubMed: 17924661
DOI: 10.1021/bi7010527
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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