1E3O

Crystal structure of Oct-1 POU dimer bound to MORE

Summary for 1E3O

• Entry DOI: 10.2210/pdb1e3o/pdb
• Related: 1CQT 1OCT 1POG
• Descriptor: 5'-D(*AP*TP*GP*CP*AP*TP*GP*AP*GP*GP*A)-3', 5'-D(*TP*CP*CP*TP*CP*AP*TP*GP*CP*AP*T)-3', OCTAMER-BINDING TRANSCRIPTION FACTOR 1, ... (4 entities in total)
• Functional Keywords: transcription, pou domain, dimer, dna binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 25105.30

Authors

Remenyi, A.,Tomilin, A.,Pohl, E.,Schoeler, H.,Wilmanns, M. (deposition date: 2000-06-20, release date: 2001-11-10, Last modification date: 2023-12-13)

Primary citation

Remenyi, A.,Tomilin, A.,Pohl, E.,Lins, K.,Philippsen, A.,Reinbold, R.,Scholer, H.R.,Wilmanns, M.
Differential Dimer Activities of the Transcription Factor Oct-1 by DNA-Induced Interface Swapping
Mol.Cell, 8:569-, 2001

PubMed 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.

PubMed: 11583619
DOI: 10.1016/S1097-2765(01)00336-7

Experimental method

X-RAY DIFFRACTION (1.9 Å)