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5KRB

GCNF DNA Binding Domain - Oct4 DR0 Complex

Summary for 5KRB
Entry DOI10.2210/pdb5krb/pdb
DescriptorDNA (5'-D(*AP*GP*AP*GP*GP*TP*CP*AP*AP*GP*GP*CP*TP*AP*GP*A)-3'), Nuclear receptor subfamily 6 group A member 1, DNA (5'-D(*TP*CP*TP*AP*GP*CP*CP*TP*TP*GP*AP*CP*CP*TP*CP*T)-3'), ... (5 entities in total)
Functional Keywordsnuclear receptor, transcription factor, dna binding, development, protein-dna complex, transcription-dna complex, transcription/dna
Biological sourceMus musculus (Mouse)
More
Total number of polymer chains4
Total formula weight29553.16
Authors
Weikum, E.R.,Ortlund, E.A. (deposition date: 2016-07-07, release date: 2016-11-09, Last modification date: 2024-04-03)
Primary citationWeikum, E.R.,Tuntland, M.L.,Murphy, M.N.,Ortlund, E.A.
A Structural Investigation into Oct4 Regulation by Orphan Nuclear Receptors, Germ Cell Nuclear Factor (GCNF), and Liver Receptor Homolog-1 (LRH-1).
J. Mol. Biol., 428:4981-4992, 2016
Cited by
PubMed Abstract: Oct4 is a transcription factor required for maintaining pluripotency and self-renewal in stem cells. Prior to differentiation, Oct4 must be silenced to allow for the development of the three germ layers in the developing embryo. This fine-tuning is controlled by the nuclear receptors (NRs), liver receptor homolog-1 (LRH-1) and germ cell nuclear factor (GCNF). Liver receptor homolog-1 is responsible for driving the expression of Oct4 where GCNF represses its expression upon differentiation. Both receptors bind to a DR0 motif located within the Oct4 promoter. Here, we present the first structure of mouse GCNF DNA-binding domain in complex with the Oct4 DR0. The overall structure revealed two molecules bound in a head-to-tail fashion on opposite sides of the DNA. Additionally, we solved the structure of the human LRH-1 DNA-binding domain bound to the same element. We explore the structural elements that govern Oct4 recognition by these two NRs.
PubMed: 27984042
DOI: 10.1016/j.jmb.2016.10.025
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.101 Å)
Structure validation

237735

数据于2025-06-18公开中

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