Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Hydrogen-deuterium exchange mass spectrometry analysis of the CDK2-cyclin A-CDC25A complex

ABSTRACT: The cell division cycle 25 phosphatases CDC25A, B and C regulate cell cycle transitions by dephosphorylating residues in the conserved glycine-rich loop of cyclin-dependent protein kinases (CDKs) to activate CDK activity. Here, we present HDX-MS data to complement the cryogenic-electron microscopy (cryo-EM) structure of CDK2-cyclin A in complex with CDC25A, providing a detailed structural analysis of the overall complex architecture and key protein-protein interactions that underpin this 86 kDa complex. This work improves our understanding of the roles of CDC25 phosphatases in CDK regulation and may inform the development of CDC25-targeting anticancer strategies.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Antonio Calabrese

LAB HEAD: Jane Endicott

PROVIDER: PXD050866 | Pride | 2024-05-29

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	both.DnX	Other
	cdc25a.DnX	Other
	fbsjrau_200817I_HDX_svitlana_cdc25a_03.raw.zip	Raw
	fbsjrau_200817I_HDX_svitlana_cdc25a_05.raw.zip	Raw
	fbsjrau_200817I_HDX_svitlana_cdc25a_07.raw.zip	Raw

Items per page:

1 - 5 of 68

Similar Datasets

Tension mediated mechanical activation and pocket delipidation lead to an analogous MscL channel state

Project description:We present HDX-MS data of WT and L89W TbMscL to interrogate the mechanism of molecular activation in this mechanosensitive channel.

2022-06-07 | PXD021983 | Pride

Mapping of a N-terminal alpha-helix domain required for human PINK1 stabilisation, Serine228 autophosphorylation and activation in cells

Project description:Comparative hydrogen deuterium exchange mass spectrometry of WT and I507A mutant for above titled manuscript.

2022-02-17 | PXD030382 | Pride

Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients revealed by HDX-MS

Project description:We present HDX-MS data of apo-SurA, SurA in complex with OmpX, OmpF and a peptide with sequence WEYIPNV to define (1) interdomain dynamics in the periplasmic chaperone SurA, and (2) the binding site of OmpX, OmpF and WEYIPNV on SurA.

2020-05-22 | PXD017010 | Pride

Fusidic acid resistance through changes in the dynamics of EF-G

Project description:HDX-MS was used to study the binding of FusB to EF-G

2020-10-15 | PXD017491 | Pride

HDX-MS of alpha-synuclein oligomers

Project description:Here we have used HDX-MS to investigate the change in structure/dynamics in synuclein oligomers formed under different conditions.

2024-05-24 | PXD038573 | Pride

Cyclic ion mobility for hydrogen/deuterium exchange-mass spectrometry applications

Project description:Hydrogen/deuterium exchange-mass spectrometry (HDX-MS) has emerged as a powerful tool to probe protein dynamics. As a bottom-up technique, HDX-MS provides information at peptide-level resolution, allowing structural localisation of dynamic changes. Consequently, HDX-MS data quality is largely determined by the number of peptides that are identified and monitored after deuteration. Integration of ion mobility (IM) into HDX-MS workflows has been shown to increase data quality by providing an orthogonal mode of peptide ion separation in the gas-phase. This is of critical importance for challenging targets such as integral membrane proteins (IMPs), which often suffer from low sequence coverage and/or redundancy in HDX-MS analyses. The increasing complexity of samples being investigated by HDX-MS, such as membrane mimetic reconstituted and in vivo IMPs, has generated need for instrumentation with greater resolving power. Recently, Giles et al. developed cyclic ion mobility (cIM), an IM device with racetrack geometry that enables scalable, multi-pass IM separations. Using 1-pass and multi-pass cIM routines, we use the recently commercialised SELECT SERIES™ Cyclic™ IM spectrometer for HDX-MS analyses of 4 detergent solubilised IMP samples and report its enhanced performance. Furthermore, we develop a novel processing strategy capable of better handling multi-pass cIM data. Interestingly, use of 1-pass and multi-pass cIM routines produced unique peptide populations, with their combined peptide output being 31 to 222% higher than previous generation SYNAPT G2-Si instrumentation. Thus, we propose a novel HDX-MS workflow with integrated cIM which has the potential to enable the analysis of more complex systems with greater accuracy and speed.

2024-04-08 | PXD048293 | Pride

HDX-MS of NicA2 and a NicA2 variant with increased activity

Project description:Here we have used HDX-MS to investigate the change in structure/dynamics in NicA2 and a variant with increased activity (v321) that was generated using directed evolution

2023-11-16 | PXD037151 | Pride

Affimer reagents as tools to modulate GPVI-ligand interactions

Project description:We have isolated Affimers that bind to GPVI and characterized their effect on receptor function. An affimer that binds specifically to dimeric GPVI was identified as a novel tool to detect dimeric GPVI. The binding sites of the different Affimers were mapped using HDX-MS, revealing that they interact with functional regions for regulating collagen binding and dimerization.

2024-10-01 | PXD046982 | Pride

Binding of a bovine ultralong CDRH3 to the SARS-CoV RBD

Project description:Here, we have used a SARS-naïve, bovine ultralong CDRH3 library to isolate a bovine paratope that engages the SARS-CoV and SARS-CoV-2 receptor-binding domain (RBD). This scFv (B9-scFv) neutralises viruses pseudo-typed with SARS-CoV Spike protein. Using differential hydrogen-deuterium exchange mass spectrometry and site-directed mutagenesis, we demonstrate that this CDRH3 recognises a conserved, cryptic epitope.

2023-03-11 | PXD032965 | Pride

HDX-MS data of BAM and SurA binding

Project description:We present HDX-MS data of the BAM:SurA complex to define the interaction sites for SurA on BAM and vice versa.

2022-07-12 | PXD030268 | Pride