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Article

Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease.

The Journal of biological chemistry - 19 Nov 2004

Ren Yan-Guo, Kirsebom Leif A, Virtanen Anders

Abstract excerpt

Poly(A)-specific ribonuclease (PARN) is a highly poly(A)-specific 3'-exoribonuclease that efficiently degrades mRNA poly(A) tails. PARN belongs to the DEDD family of nucleases, and four conserved residues are essential for PARN activity, i.e. Asp-28, Glu-30, Asp-292, and Asp-382. Here we have investigated how catalytically important divalent metal ions are coordinated in the active site of PARN. Each of the...

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Source

Identifiers

PMID: 15358788
DOI: 10.1074/jbc.M403858200

Genes

PARN
DEDD

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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