National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
HD8818
United States
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
HD07857
United States
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
NIDDK59820
United States
Welch Foundation
Q-1967-20180324
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM143380
United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
R01HL162842
United States
Department of Defense (DOD, United States)
DAMD W81WH-21-1-0404
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM080139
United States
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
R01HD042311
United States
Citation
Journal: iScience / Year: 2022 Title: Spatial definition of the human progesterone receptor-B transcriptional complex. Authors: Xinzhe Yu / Ping Yi / Anil K Panigrahi / Lance Edward V Lumahan / John P Lydon / David M Lonard / Steven J Lutdke / Zhao Wang / Bert W O'Malley / Abstract: We report the quaternary structure of core transcriptional complex for the full-length human progesterone receptor-B (PR-B) homodimer with primary coactivator steroid receptor coactivator-2 (SRC-2) ...We report the quaternary structure of core transcriptional complex for the full-length human progesterone receptor-B (PR-B) homodimer with primary coactivator steroid receptor coactivator-2 (SRC-2) and the secondary coactivator p300/CREB-binding protein (CBP). The PR-B homodimer engages one SRC-2 mainly through its activation function 1 (AF1) in N-terminus. SRC-2 is positioned between PR-B and p300 leaving space for direct interaction between PR-B and p300 through PR-B's C-terminal AF2 and its unique AF3. Direct AF3/p300 interaction provides long-desired structural insights into the known functional differences between PR-B and the PR-A isoform lacking AF3. We reveal the contributions of each AF and demonstrate their structural basis in forming the PR-B dimer interface and PR-B/coactivator complex. Comparison of the PR-B/coactivator complex with other steroid receptor (estrogen receptor and androgen receptor) complexes also shows that each receptor has its unique mechanism for recruiting coactivators due to the highly variable N-termini among receptors.
Name: PRE-DNA/PR-B complex / type: complex / ID: 1 / Parent: 0 / Details: Progesterone Receptor and DNA complex
Source (natural)
Organism: Homo sapiens (human)
Molecular weight
Theoretical: 370 KDa
-
Experimental details
-
Structure determination
Method
cryo EM
Processing
single particle reconstruction
Aggregation state
particle
-
Sample preparation
Concentration
0.01 mg/mL
Buffer
pH: 7.5
Grid
Model: Quantifoil R1.2/1.3 / Material: COPPER
Vitrification
Cryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 291 K / Instrument: FEI VITROBOT MARK IV
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Electron microscopy
Microscope
TFS GLACIOS
Image recording
Film or detector model: FEI FALCON IV (4k x 4k) / Detector mode: SUPER-RESOLUTION / Number real images: 7011 / Average exposure time: 8.0 sec. / Average electron dose: 55.0 e/Å2
Electron beam
Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
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