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Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state

ABSTRACT: Detailed characterization of PPM1D phosphatase by HDX-MS: conformational dynamics of the pathogenic truncated form (1-420) found in various cancers, the effect of different truncations and mutations and mapping an inhibitor binding site.

INSTRUMENT(S): Xevo G2 XS QToF (Waters)

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Benjamin Ebert Colin Garvie

PROVIDER: MSV000088711 | MassIVE | Thu Jan 20 22:00:00 GMT 2022

REPOSITORIES: MassIVE

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Allosteric inhibition of PPM1D serine/threonine phosphatase via an altered conformational state.

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Activation loop phosphorylation tunes conformational dynamics underlying Pyk2 tyrosine kinase activation

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The conformational state of PLCγ cSH2-linker contributes to Ibrutinib resistance

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