1GT0

Crystal structure of a POU/HMG/DNA ternary complex

Summary for 1GT0

• Entry DOI: 10.2210/pdb1gt0/pdb
• Related: 1CQT 1E3O 1HF0 1OCT 1POG 1POU
• Descriptor: 5'-D(*TP*TP*CP*TP*TP*TP*GP*TP*TP*TP* GP*GP*AP* TP*GP*CP*TP*AP*AP*TP*GP*GP*GP*A)-3', 5'-D(*AP*TP*CP*CP*CP*AP*TP*TP*AP*GP* CP*AP*TP*CP*CP*AP*AP*AP*CP*AP*AP*AP*GP*A)-3', OCTAMER-BINDING TRANSCRIPTION FACTOR 1, ... (5 entities in total)
• Functional Keywords: transcription factor, pou factors, sox proteins, transcription
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 4
• Total formula weight: 42897.90

Authors

Remenyi, A.,Wilmanns, M. (deposition date: 2002-01-09, release date: 2003-01-30, Last modification date: 2024-05-08)

Primary citation

Remenyi, A.,Lins, K.,Nissen, L.J.,Reinbold, R.,Scholer, H.R.,Wilmanns, M.
Crystal Structure of a POU/Hmg/DNA Ternary Complex Suggests Differential Assembly of Oct4 and Sox2 on Two Enhancers
Genes Dev., 17:2048-, 2003

PubMed Abstract: Members of the POU and SOX transcription factor families exemplify the partnerships established between various transcriptional regulators during early embryonic development. Although functional cooperativity between key regulator proteins is pivotal for milestone decisions in mammalian development, little is known about the underlying molecular mechanisms. In this study, we focus on two transcription factors, Oct4 and Sox2, as their combination on DNA is considered to direct the establishment of the first three lineages in the mammalian embryo. Using experimental high-resolution structure determination, followed by model building and experimental validation, we found that Oct4 and Sox2 were able to dimerize onto DNA in distinct conformational arrangements. We demonstrate that the DNA enhancer region of their target genes is responsible for the correct spatial alignment of glue-like interaction domains on their surface. Interestingly, these surfaces frequently have redundant functions and are instrumental in recruiting various interacting protein partners.

PubMed: 12923055
DOI: 10.1101/GAD.269303

Experimental method

X-RAY DIFFRACTION (2.6 Å)