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Article

Structural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolase.

Nature communications - 1 Jan 2013

Zhu Chunfeng, Gao Wenying, Zhao Ke, Qin Xiaohong, Zhang Yinjie, Peng Xin, Zhang Lei, Dong Yuhui, Zhang Wenyan, Li Peng, Wei Wei, Gong Yong, Yu Xiao-Fang

Abstract excerpt

SAMHD1 is a dGTP-activated deoxynucleoside triphosphate triphosphohydrolase (dNTPase) whose dNTPase activity has been linked to HIV/SIV restriction. The mechanism of its dGTP-activated dNTPase function remains unclear. Recent data also indicate that SAMHD1 regulates retrotransposition of LINE-1 elements. Here we report the 1.8-Å crystal structure of homotetrameric SAMHD1 in complex with the allosteric activator...

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Identifiers

PMID: 24217394
DOI: 10.1038/ncomms3722

Genes

SAMHD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Structural insight into dGTP-dependent activation of tetrameric SAMHD1 deoxynucleoside triphosphate triphosphohydrolase.PMID 24217394Read ↗

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