5L0M

hLRH-1 DNA Binding Domain - 12bp Oct4 promoter complex

Summary for 5L0M

• Entry DOI: 10.2210/pdb5l0m/pdb
• Descriptor: Nuclear receptor subfamily 5 group A member 2, DNA (5'-D(*CP*TP*AP*GP*CP*CP*TP*TP*GP*AP*CP*C)-3'), DNA (5'-D(*GP*GP*TP*CP*AP*AP*GP*GP*CP*TP*AP*G)-3'), ... (6 entities in total)
• Functional Keywords: lrh-1, nuclear receptor, oct4, dbd, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 20701.04

Authors

Tuntland, M.L.,Ortlund, E.A. (deposition date: 2016-07-27, release date: 2016-11-09, Last modification date: 2023-10-04)

Primary citation

Weikum, 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

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

Experimental method

X-RAY DIFFRACTION (2.197 Å)