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Dynamics of allosteric regulation of the phospholipase C-gamma isoform

ABSTRACT: we used hydrogen deuterium exchange masss spec (HDX-MS) to define the exchange kinetics of PLC-y1 as it interacts with the kinase domain of FGFR1, and liposomes containing PIP2, in order to understand how PLC-y isozymes operate at membranes. We show that the binding of FGFR1k to PLC-y1 increases deuterium incorporation within the interface between the regulatory domains and the catalytic core. Importantly, the addition of liposomes further increase deuterium exchange within the same region.

INSTRUMENT(S): impact HD

ORGANISM(S): Rattus Norvegicus (rat)

SUBMITTER: John Burke

LAB HEAD: Dr John E Burke

PROVIDER: PXD030492 | Pride | 2022-06-14

REPOSITORIES: Pride

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			Action	DRS
	01042019_RHHDX22_PLC_D1165H_CD_MSMS_25pmol_DBSEARCH_7.zip	Other
	01042019_RHHDX22_PLC_WT_and_D1165H__-peptide_-Lipid_-FGFR.hdx	Other
	01042019_RHHDX22_PLC_WT_and_D1165H__-peptide_-Lipid_-FGFR_MutationPeptidesOnly.hdx	Other
	01_4_19_RHHDX22_PLC_A_30s_1_0_01_9572.d.zip	Other
	01_4_19_RHHDX22_PLC_B_30s_1_0_01_9574.d.zip	Other

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