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Molecular determinant for MED1 interaction with the VDR-RXR heterodimer

ABSTRACT: To provide structural insights into the mechanism of the specific association of the coactivator MED1 with the Vitamin D nuclear (VDR)-RXR heterodimer, we used combined structural methods including X-ray crystallography, small angle X-ray scattering (SAXS), NMR, hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS), crosslinking mass spectrometry as well as biophysical methods.

INSTRUMENT(S): Exactive Plus, SYNAPT G2-Si

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Maxime BOURGUET

LAB HEAD: Sarah Cianferani

PROVIDER: PXD019530 | Pride | 2021-02-10

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Cluster_data.zip	Other
	Dataset_MED1.zip	Other
	Dataset_VDR_RXR.zip	Other
	Dataset_VDR_RXR_MED1.zip	Other
	Dataset_VDR_RXR_MED1_XL-MS.zip	Other

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Publications

Molecular determinants of MED1 interaction with the DNA bound VDR-RXR heterodimer.

Belorusova Anna Y AY Bourguet Maxime M Hessmann Steve S Chalhoub Sandra S Kieffer Bruno B Cianférani Sarah S Rochel Natacha N

Nucleic acids research 20201101 19

The MED1 subunit of the Mediator complex is an essential coactivator of nuclear receptor-mediated transcriptional activation. While structural requirements for ligand-dependent binding of classical coactivator motifs of MED1 to numerous nuclear receptor ligand-binding domains have been fully elucidated, the recognition of the full-length or truncated coactivator by full nuclear receptor complexes remain unknown. Here we present structural details of the interaction between a large part of MED1 c ...[more]

PMID: 32990725

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Structural basis for DNA recognition and allosteric control of the Retinoic Acid Receptors RAR-RXR

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HDX-MS Analysis of CD47 Conformational Dynamics

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