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Article

A structural basis for lithium and substrate binding of an inositide phosphatase.

The Journal of biological chemistry - 1 Jan 2000

Dollins D Eric, Xiong Jian-Ping, Endo-Streeter Stuart, Anderson David E, Bansal Vinay S, Ponder Jay W, Ren Yi, York John D

Abstract excerpt

Inositol polyphosphate 1-phosphatase (INPP1) is a prototype member of metal-dependent/lithium-inhibited phosphomonoesterase protein family defined by a conserved three-dimensional core structure. Enzymes within this family function in distinct pathways including inositide signaling, gluconeogenesis, and sulfur assimilation. Using structural and biochemical studies, we report the effect of substrate and lithium on...

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Identifiers

PMID: 33172890
DOI: 10.1074/jbc.RA120.014057
PMCID: PMC7948987

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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