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ProteomicsMolecular determinant for MED1 interaction with the VDR-RXR heterodimer
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 t...
ORGANISM(S): Homo sapiens (Human) 
2021-02-10 | PXD019530 | Pride
Nuclear receptor Vdr-rxr Xl-ms Hdx-ms 
ProteomicsBacillus subtilis RNase M5 cleaves dsRNA in two steps via a two Mg2+-ion dependent mechanism
Here, we present the crystal structure of the catalytic domain of M5 bound to two magnesium ions, which reveals the role of each catalytic site acidic residue in metal binding. We further use hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS) to investigate the possibility of structur...
ORGANISM(S): Geobacillus stearothermophilus 
2021-02-10 | PXD019202 | Pride
Rnase Native-ms Hdx-ms 
ProteomicsStructural basis for DNA recognition and allosteric control of the Retinoic Acid Receptors RAR-RXR
Retinoic Acid Receptors (RARs) as a functional heterodimer with Retinoid X Receptors (RXRs), bind a diverse series of RA-response elements (RAREs) in regulated genes. Among them, the non-canonical DR0 elements are bound by RXR-RAR with comparable affinities to DR5 elements but DR0 elements do not ac...
ORGANISM(S): Mus musculus (Mouse) 
2021-02-10 | PXD018172 | Pride
Hdx Nuclear receptors Structural ms Hdx-ms 
ProteomicsPervanadate mediated cysteine oxidation directly activates SRC kinase
Protein tyrosine phosphorylation (pTyr) is regulated by protein tyrosine phosphatases (PTPs) and27 kinases, helping cells detect and react to environmental changes. Pervanadate is commonly used to increase pTyr levels by inhibiting PTPs, leading to the belief that PTPs are the main regulators of pTy...
ORGANISM(S): Homo sapiens (Human) 
2026-02-05 | PXD059840 | Pride
Src Oxidation Kinase Hdx-ms 
ProteomicsA novel RAB5 binding site in human VPS34-CII that is likely the primordial site in eukaryotic evolution
RAB5-GTP activation of the multiprotein VPS34 complex II (VPS34-CII) is critical for endosomal sorting and maturation, phagocytosis, and receptor downregulation. RAB5-GTP activates VPS34-CII, by binding to a helical insertion in the C2 domain of VPS34 on the BECLIN1/UVRAG-containing adaptor arm of t...
ORGANISM(S): Homo sapiens (Human) 
2026-05-26 | PXD061277 | Pride
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