Proteomics

Dataset Information

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HDX-MS analysis of hPLCγ1 binding interactions with a small molecule compound

ABSTRACT: We used HDX-MS to map potential binding sites of a small molecule compund on hPLCγ1. We identified multiple sites which show a conformational change upon ligand binding indicating this compund is able to interact with hPLCγ1.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD051153 | Pride | 2025-10-15

REPOSITORIES: pride

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Dataset's files

Source:
Action DRS
01_09_24_HN9_CB_0.3s-1.d.rar Other
01_09_24_HN9_PL_0.3s-1.d.rar Other
01_10_24_HN9_CB_300s-1.d.rar Other
01_10_24_HN9_PL_300s-1.d.rar Other
01_10_24_HN9_PL_30s-1.d.rar Other
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Publications

Characterisation of an allosteric site in PLCγ enzymes and implications for development of their specific inhibitors.

Bunney Tom D TD   Nyvall Hunter G HG   Macrae Calum C   Lalović Damjan D   Gregory Ashley A   Le Huray Kyle I P KIP   Harvey Nikita N   Pinotsis Nikos N   Kalli Antreas C AC   Waudby Christopher A CA   Burke John E JE   Katan Matilda M  

The Biochemical journal 20251016 20

Phospholipase C gamma (PLCγ) enzymes are key components of intracellular signal transduction processes and are involved in disease development, including immune dysregulation, specific cancer types and neurodegeneration. Although recognised as important targets for intervention, validated pharmacological tools are lacking. Here, we demonstrate that inhibitory nucleotides bind directly to an allosteric site at the interface between the PLC-core and regulatory-array unique for PLCγ, underlying the  ...[more]

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