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Article

Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions.

Scientific reports - 1 Mar 2016

Yokogawa Mariko, Tsushima Takashi, Noda Nobuo N, Kumeta Hiroyuki, Enokizono Yoshiaki, Yamashita Kazuo, Standley Daron M, Takeuchi Osamu, Akira Shizuo, Inagaki Fuyuhiko

Abstract excerpt

Regnase-1 is an RNase that directly cleaves mRNAs of inflammatory genes such as IL-6 and IL-12p40, and negatively regulates cellular inflammatory responses. Here, we report the structures of four domains of Regnase-1 from Mus musculus-the N-terminal domain (NTD), PilT N-terminus like (PIN) domain, zinc finger (ZF) domain and C-terminal domain (CTD). The PIN domain harbors the RNase catalytic center; however, it...

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Identifiers

PMID: 26927947
DOI: 10.1038/srep22324
PMCID: PMC4772114

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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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