PDBsum entry 2h8r

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protein dna_rna Protein-protein interface(s) links
Transcription activator/DNA PDB id
Protein chains
176 a.a. *
Waters ×7
* Residue conservation analysis
PDB id:
Name: Transcription activator/DNA
Title: Hepatocyte nuclear factor 1b bound to dna: mody5 gene product
Structure: Hepatocyte nuclear factor 1-beta. Chain: a, b. Fragment: DNA binding domain (residues 91-310). Synonym: hnf-1beta, hnf-1b, variant hepatic nuclear factor 1, vhnf1, homeoprotein lfb3, transcription factor 2, tcf-2. Engineered: yes. 5'- d( Cp Tp Tp Gp Gp Tp Tp Ap Ap Tp Ap Ap Tp Tp Cp Ap Cp Cp Ap G)-3'.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Synthetic: yes
3.20Å     R-factor:   0.226     R-free:   0.290
Authors: P.Lu,G.B.Rha,Y.I.Chi
Key ref: P.Lu et al. (2007). Structural basis of disease-causing mutations in hepatocyte nuclear factor 1beta. Biochemistry, 46, 12071-12080. PubMed id: 17924661
07-Jun-06     Release date:   19-Jun-07    
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Protein chains
Pfam   ArchSchema ?
P35680  (HNF1B_HUMAN) -  Hepatocyte nuclear factor 1-beta
557 a.a.
176 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of transcription, DNA-dependent   2 terms 
  Biochemical function     DNA binding     3 terms  


Biochemistry 46:12071-12080 (2007)
PubMed id: 17924661  
Structural basis of disease-causing mutations in hepatocyte nuclear factor 1beta.
P.Lu, G.B.Rha, Y.I.Chi.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18829458 P.Lu, G.B.Rha, M.Melikishvili, G.Wu, B.C.Adkins, M.G.Fried, and Y.I.Chi (2008).
Structural Basis of Natural Promoter Recognition by a Unique Nuclear Receptor, HNF4{alpha}: DIABETES GENE PRODUCT.
  J Biol Chem, 283, 33685-33697.
PDB code: 3cbb
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