Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A metzincin-like O-glycopeptidase from Akkermansia muciniphila requires the Tn antigen for cleavage of the peptide bond.

ABSTRACT: HDX-MS analysis of the protein ALT51, comparing deuterium uptake between the full length protein and a truncated construct missing the CBM-like domain. Mass spectrometry was used to map the cleavage sites of CAT in a selection of representitive mucin-like glycoproteins.

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD034904 | Pride | 2022-08-31

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Structure of the phosphoinositide 3-kinase p110-p101 complex reveals molecular mechanism of GPCR activation

Project description:The class IB phosphoinositide 3-kinase (PI3K), PI3K, is a master regulator of immune cell function, and is a promising drug target for both inflammatory diseases and cancer. Critical to PI3K function is the association of the p110 catalytic subunit to either a p101 or p84 regulatory subunit, which mediates regulation by G-protein coupled receptors (GPCRs). Here, we report the first structure of a heterodimeric PI3K complex, p110-p101. This structure revealed a unique mode of assembly of catalytic and regulatory subunits distinct from that of other class I PI3K complexes. Multiple oncogenic mutations mapped to these novel interfaces led to increased activation by G. p101 mediates activation through its G binding domain, recruiting the complex to the membrane and allowing for engagement of a secondary site in p110. A nanobody that specifically binds to this p101-G interface blocks activation providing a novel tool to study p101-specific signaling events in vivo.

2021-09-22 | PXD025209 | Pride

HDX-MS Analysis of CeSpartin and CtSpartinL

Project description:HDX-MS analysis of SPG20, determining the seconday structure of CeSpartin and comparing WT CtSpartinL and A290P CtSpartinL.

2023-12-27 | PXD043175 | Pride

ATP-competitive and allosteric inhibitors induce differential conformational changes at the autoinhibitory interface of Akt

Project description:We use HDX-MS to interrogate the AKT1 DrLink conformational changes upon binding AKT1 active site inhibitors A-443654, Capivasertib, and Uprosertib, Akt1 allosteric inhibitor MK-2206, and ADP.

2024-08-23 | PXD039028 | Pride

Detailing the Structural and Dynamic Interactions Between WDR44 and Rab11

Project description:DR44 is a Rab11 effector protein that is thought to regulate ciliogenesis by competing with pro-ciliogenesis factors for Rab11 binding. The structure of WDR44 and the molecular mechanism of its interaction with Rab11 is unknown. To explore the interactions between these two proteins multiple WDR44 constructs were designed and pulled down with Rab11. Using the results of the pulldown assay as a guide we used protein complex prediction software, and hydrogen deuterium exchange mass spectrometry (HDX-MS) to identify the binding interface between WDR44 and Rab11. Mutagenesis was used to make specific mutations in the putative Rab11 binding region of WDR44.

2023-03-11 | PXD035741 | Pride

HDX-MS analysis of PI4Ka trimer and FAM126a (415-521) with calcineurin

Project description:We used HDX-MS to map novel binding sites of calcineurin on PI4KA and FAM126A. Calcineurin binds to PxIxIT and LxVP motifs on PI4KA and FAM126A indicating a novel regulatory mechanism of Pi4KA by calcineurin

2024-09-03 | PXD050633 | Pride

HDX-MS Analysis of the protein ALT51

Project description:HDX-MS analysis of the protein ALT51, comparing deuterium uptake between the full length protein and a truncated construct missing the CBM-like domain

2023-02-22 | PXD034850 | Pride

Defining the molecular mechanism of PI4KA complex regulation by the phosphatase Calcineurin

Project description:To examine the interaction between PI4KIIIa and Calcineurin, HDX-MS experiments comparing calcineurin or PI4KA FAM delta C alone to the calcineurin and PI4KA FAM delta C complex were carried out.

2024-09-03 | PXD043409 | Pride

Hydrogen Deuterium Exchange of PI4K(530-560) Peptide with Calcineurin

Project description:we used HDXMS to study if PI4KA(530-560) is able to bind calcineurin. Here we showed a significant protection in deuterium exchange upon binding calcineurin in the wild type state, indicating these proteins are interacting. Using a mutant that should inhibit the interaction (AKASAA), we showed that this mutant does in fact prevent protection by calcineurin.

2024-09-03 | PXD044636 | Pride

Hydrogen Deuterium Exchange of PDK1

Project description:This project consisted of three HDX-MS experiments. First, we compared the dimeric PDK1(SKD-PIF) to monomeric PDK1(SKD) and mapped the differences in deuterium incorporation onto the dimer model. We then compared the deuterium incorporation kinetics for the kinase (PDK1(SKD)) and PH (PDK1(PH) domains of PDK1 with full-length PDK1 (PDK1(FL)) in pairwise experiments.

2022-05-20 | PXD027401 | Pride

HDX-MS analysis of PLIN3 membrane binding

Project description:Hydrogen deuterium exchange mass spectrometry of PLIN3 in the presence of three different membrane vesicles to analyze structural changes induced by membrane binding.

2023-04-14 | PXD025717 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data