National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
HD8818
米国
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
HD07857
米国
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
NIDDK59820
米国
Welch Foundation
Q-1967-20180324
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM143380
米国
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
R01HL162842
米国
Department of Defense (DOD, United States)
DAMD W81WH-21-1-0404
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM080139
米国
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)
R01HD042311
米国
引用
ジャーナル: iScience / 年: 2022 タイトル: Spatial definition of the human progesterone receptor-B transcriptional complex. 著者: 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 / 要旨: 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.