Summary information and primary citation
- PDB-id
-
1hf0;
DSSR-derived features in text and
JSON formats
- Class
- transcription
- Method
- X-ray (2.7 Å)
- Summary
- Crystal structure of the DNA-binding domain of oct-1
bound to DNA as a dimer
- Reference
-
Remenyi A, Tomilin A, Pohl E, Lins K, Philippsen A,
Reinbold R, Scholer HR, Wilmanns M (2001): "Differential
Dimer Activities of the Transcription Factor Oct-1 by
DNA-Induced Interface Swapping." Mol.Cell,
8, 569. doi: 10.1016/S1097-2765(01)00336-7.
- Abstract
- 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.
