Nathalie Sibille
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nsibille.bsky.social
Nathalie Sibille
@nsibille.bsky.social
PhD in Biophysics, CNRS research director, team leader at Montpellier University
NMR spectroscopist, structural biologist & IDPs, phosphorylation, PTMs, GPCRs and cell signaling lover
Reposted by Nathalie Sibille
LIPIDS MODULATE THE DYNAMICS OF GPCR:β-ARRESTIN INTERACTION https://www.biorxiv.org/content/10.1101/2024.03.16.585329v1
LIPIDS MODULATE THE DYNAMICS OF GPCR:β-ARRESTIN INTERACTION https://www.biorxiv.org/content/10.1101/2024.03.16.585329v1
{beta}-arrestins are key privileged molecular partners of G-Protein Coupled Receptors (GPCRs), trigg
www.biorxiv.org
March 17, 2024 at 7:49 PM
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December 17, 2024 at 2:06 PM
It's fantastic to see our latest results in @Structure_CP, highligted by @irenecoin and Daniel Huster, in the fascinating world of @GPCR, @IDPs, and @NMR. Congratulations to my team @CNRS @umontpellier 🥳👏, funded by @AgenceRecherche GPCteR. Thank you 🙌🔬

doi.org/10.1016/j.str.…
January 7, 2025 at 7:53 PM
Very happy to share our last results in @Structure on @GPCR, @IDPs & @NMR at @CNRS and @UniversityMontpellier with the support of #ANR GPCteR. Congratulations to my team 👏 @Myriam Guillien and @AssiaMouhand, @AminSagar1 and all involved in the project.

sciencedirect.com/science/articl…
January 7, 2025 at 7:53 PM
Very happy to share our last results on the #ANR GPCteR project at #CNRS. Congrats to my team 👏 : @myriamguillien, @AssiaMouhand, @AminSagar1

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January 7, 2025 at 7:53 PM
Structural insights into the cooperative interaction of the intrinsically disordered co-activator TIF2 with retinoic acid receptor heterodimer (RXR/RAR

biorxiv.org/content/10.110…
Structural insights into the cooperative interaction of the intrinsically disordered co-activator TIF2 with retinoic acid receptor heterodimer (RXR/RAR)
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 (TIF2NRID) 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 TIF2NRID by integrating several experimental (NMR, SAXS, 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 TIF2NRID in complex with RXR/RAR reveal a cooperative binding of the three NR-boxes as well as an active role of their flanking regions in the interaction. ### Competing Interest Statement The authors have declared no competing interest.
www.biorxiv.org
January 7, 2025 at 7:53 PM