Related Experiment Video
Updated: Aug 17, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
Published on: April 26, 2013
The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda
N Assa-Munt1, R J Mortishire-Smith, R Aurora
1Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037.
Abstract:
The POU-specific (POUs) domain, in association with a POU-type homeodomain, forms the bipartite DNA-binding POU domain. The solution structure of the Oct-1 POUs domain has been determined by multidimensional nuclear magnetic resonance spectroscopy and consists of four alpha helices surrounding a conserved hydrophobic core. The POUs domain is structurally similar to the DNA-binding domains of the bacteriophage lambda and 434 repressors and 434 Cro. These domains exhibit superimposable helix-turn-helix (HTH) motifs, except that in the POUs domain, the first helix and the linker to the second helix of the motif are extended. The conserved structural features have been used to propose a plausible model for DNA binding by the POUs domain. A human dwarfism mutation that affects positive control in the related POU domain protein Pit-1 maps to the same region of the HTH motif as do positive control mutations in lambda repressor.
More Related Videos
Related Concept Videos
DNA Topoisomerases
Types and Mechanism of action
Topoisomerases are divided into two main types. Type I...
Cooperative Binding of Transcription Regulators
Single-Strand DNA Binding Proteins
DNA Bacteriophages
Inhibitors of Bacterial DNA Synthesis

