Proteomics

Dataset Information

0

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

Dataset's files

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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]

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