2H8R
Hepatocyte Nuclear Factor 1b bound to DNA: MODY5 Gene Product
Summary for 2H8R
Entry DOI | 10.2210/pdb2h8r/pdb |
Descriptor | 5'-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 Keywords | trasncription factor, pou, homeo, protein-dna, human disease, transcription activator-dna complex, transcription activator/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: P35680 |
Total number of polymer chains | 4 |
Total formula weight | 63688.69 |
Authors | |
Primary citation | Lu, 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: 17924661DOI: 10.1021/bi7010527 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
Download full validation report
