7APO
Crystal structure of RARalpha ligand binding domain in complex with a fragment of the TIF2 coactivator
Summary for 7APO
| Entry DOI | 10.2210/pdb7apo/pdb |
| Descriptor | Retinoic acid receptor alpha, Nuclear receptor coactivator 2, 4-{[(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)carbonyl]amino}benzoic acid, ... (5 entities in total) |
| Functional Keywords | nuclear hormone receptor, coactivator, transcription factor, retinoic acid, dna binding protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 63173.20 |
| Authors | le Maire, A.,Guee, L.,Bourguet, W. (deposition date: 2020-10-19, release date: 2021-08-04, Last modification date: 2024-01-31) |
| Primary citation | Senicourt, L.,le Maire, A.,Allemand, F.,Carvalho, J.E.,Guee, L.,Germain, P.,Schubert, M.,Bernado, P.,Bourguet, W.,Sibille, N. Structural Insights into the Interaction of the Intrinsically Disordered Co-activator TIF2 with Retinoic Acid Receptor Heterodimer (RXR/RAR). J.Mol.Biol., 433:166899-166899, 2021 Cited by PubMed Abstract: Retinoic acid receptors (RARs) and retinoid X receptors (RXRs) form heterodimers that activate target gene transcription by recruiting co-activator complexes in response to ligand binding. The nuclear receptor (NR) co-activator TIF2 mediates this recruitment by interacting with the ligand-binding domain (LBD) of NRs trough the nuclear receptor interaction domain (TIF2) containing three highly conserved α-helical LxxLL motifs (NR-boxes). The precise binding mode of this domain to RXR/RAR is not clear due to the disordered nature of TIF2. Here we present the structural characterization of TIF2 by integrating several experimental (NMR, SAXS, Far-UV CD, SEC-MALS) and computational data. Collectively, the data are in agreement with a largely disordered protein with partially structured regions, including the NR-boxes and their flanking regions, which are evolutionary conserved. NMR and X-ray crystallographic data on TIF2 in complex with RXR/RAR reveal a multisite binding of the three NR-boxes as well as an active role of their flanking regions in the interaction. PubMed: 33647291DOI: 10.1016/j.jmb.2021.166899 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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