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HDX-MS analysis of Lipin in the presence and absence of anionic membranes

ABSTRACT: HDX-MS analysis of Lipin binding to anionic membranes

INSTRUMENT(S): ultraflex

ORGANISM(S): Tetrahymena Thermophila Sb210

SUBMITTER: John Burke

LAB HEAD: John Burke

PROVIDER: PXD017575 | Pride | 2020-03-18

REPOSITORIES: Pride

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			Action	DRS
	11_3_19_RHHDX12_TTL_A_10000s_2_0_01_9299.d.zip	Other
	11_3_19_RHHDX12_TTL_A_3000s_2_0_01_9295.d.zip	Other
	11_3_19_RHHDX12_TTL_A_300s_3_0_01_9311.d.zip	Other
	11_3_19_RHHDX12_TTL_A_30s_3_0_01_9307.d.zip	Other
	11_3_19_RHHDX12_TTL_A_3s_3_0_01_9303.d.zip	Other

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Publications

Crystal structure of a lipin/Pah phosphatidic acid phosphatase.

Khayyo Valerie I VI Hoffmann Reece M RM Wang Huan H Bell Justin A JA Burke John E JE Reue Karen K Airola Michael V MV

Nature communications 20200311 1

Lipin/Pah phosphatidic acid phosphatases (PAPs) generate diacylglycerol to regulate triglyceride synthesis and cellular signaling. Inactivating mutations cause rhabdomyolysis, autoinflammatory disease, and aberrant fat storage. Disease-mutations cluster within the conserved N-Lip and C-Lip regions that are separated by 500-residues in humans. To understand how the N-Lip and C-Lip combine for PAP function, we determined crystal structures of Tetrahymena thermophila Pah2 (Tt Pah2) that directly fu ...[more]

PMID: 32161260

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