1HF0: Crystal Structure Of The Dna-Binding Domain Of Oct-1 Bound To Dna As A Dimer

Two crystal structures of Oct-1 POU domain bound to DNA provide a rationale for differential, conformation-dependent recruitment of transcription cofactors. The POU-homeo and POU-specific subdomains of Oct-1 contain two different nonoverlapping pairs of surface patches that are capable of forming unrelated protein-protein interfaces. Members of the POU factor family contain one or two conserved sequence motifs in the interface that are known to be phosphorylated, as noted for Oct-1 and Pit-1. Modeling of Oct-4 reveals the unique case where the same conserved sequence is located in both interfaces. Our studies provide the basis for two distinct dimeric POU factor arrangements that are dictated by the architecture of each DNA response element. We suggest interface swapping in dimers could be a general mechanism of modulating the activity of transcription factors.
PDB ID: 1HF0Download
MMDB ID: 49450
PDB Deposition Date: 2000/11/27
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1HF0: tetrameric; determined by software (PISA)
Molecular Components in 1HF0
Label Count Molecule
Proteins (2 molecules)
Octamer-binding Transcription Factor 1(Gene symbol: POU2F1)
Molecule annotation
Nucleotides(2 molecules)
DNA 5'-d(*cp*ap*cp*ap*tp*tp*tp*gp*ap*ap*ap*gp*gp* Cp*ap*ap*ap*tp*gp*gp*ap*g)-3'
Molecule annotation
DNA 5'-d(*cp*tp*cp*cp*ap*tp*tp*tp*gp*cp*cp*tp*tp* Tp*cp*ap*ap*ap*tp*gp*tp*g)-3'
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB