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Article

Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding.

The Journal of biological chemistry - 8 Oct 2004

Maynes Jason T, Perreault Kathleen R, Cherney Maia M, Luu Hue Anh, James Michael N G, Holmes Charles F B

Abstract excerpt

Protein phosphatase-1 and protein phosphatase-2B (calcineurin) are eukaryotic serine/threonine phosphatases that share 40% sequence identity in their catalytic subunits. Despite the similarities in sequence, these phosphatases are widely divergent when it comes to inhibition by natural product to...

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Identifiers

PMID: 15280359
DOI: 10.1074/jbc.M407184200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15280359-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding.PMID 15280359Read ↗

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