Proteomics

Dataset Information

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Mapping the Interaction between Eukaryotic Initiation Factor 4A (eIF4A) and the Inhibitor Hippuristanol Using Carbene Footprinting and Mass Spectrometry


ABSTRACT: Protein-ligand interactions are central to protein activity and cell functionality. Improved knowledge of these relationships greatly benefits our understanding of key biological processes and aids in rational drug design towards the treatment of clinically relevant diseases. Carbene footprinting is a recently developed mass spectrometry-based chemical labelling technique that provides valuable information relating to protein-ligand interactions, such as the mapping of binding sites and associated conformational change. Here we show the application of carbene footprinting to the interaction between eIF4A helicase and a natural product inhibitor, hippuristanol, found in the coral Isis hippuris. Upon addition of hippuristanol we identified reduced carbene labelling (masking) in regions of eIF4A previously implicated in ligand binding. Additionally, we detected hippuristanol-associated increased carbene labelling (unmasking) around the flexible hinge region of eIF4A, indicating ligand-induced conformational change. This work represents further development of the carbene footprinting technique and demonstrates its potential in characterising medicinally relevant protein-ligand interactions.

INSTRUMENT(S): LTQ FT

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: James Lloyd  

LAB HEAD: Neil J. Oldham

PROVIDER: PXD025105 | Pride | 2021-08-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ALH_eIF4A_DDA.RAW Raw
ALH_eIF4A_DDA.xml Xml
Copy_of_JRL_140120_eIF4a_CO1.RAW Raw
Copy_of_JRL_140120_eIF4a_CO2.RAW Raw
Copy_of_JRL_140120_eIF4a_CO3.RAW Raw
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Publications

Mapping the interaction between eukaryotic initiation factor 4A (eIF4A) and the inhibitor hippuristanol using carbene footprinting and mass spectrometry.

Lloyd James R JR   Hogan Amy A   Paschalis Vasileios V   Bellamy-Carter Jeddidiah J   Bottley Andrew A   Seymour Graham B GB   Hayes Christopher J CJ   Oldham Neil J NJ  

Proteomics 20210606 21-22


Protein-ligand interactions are central to protein activity and cell functionality. Improved knowledge of these relationships greatly benefits our understanding of key biological processes and aids in rational drug design towards the treatment of clinically relevant diseases. Carbene footprinting is a recently developed mass spectrometry-based chemical labelling technique that provides valuable information relating to protein-ligand interactions, such as the mapping of binding sites and associat  ...[more]

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