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Title | Spatial definition of the human progesterone receptor-B transcriptional complex. |
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Journal, issue, pages | iScience, Vol. 25, Issue 11, Page 105321, Year 2022 |
Publish date | Nov 18, 2022 |
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 / |
PubMed 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. |
External links | iScience / PubMed:36325049 / PubMed Central |
Methods | EM (single particle) |
Resolution | 10.91 - 19.1 Å |
Structure data | EMDB-27537: Spatial Definition of the Human Progesterone Receptor-B Transcriptional Complex EMDB-27540: Spatial Definition of the Human Progesterone Receptor-B Transcriptional Complex |
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