Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.

The Journal of biological chemistry - 21 Nov 2014

Koharudin Leonardus M I, Wu Ying, DeLucia Maria, Mehrens Jennifer, Gronenborn Angela M, Ahn Jinwoo

Abstract excerpt

Sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) plays a critical role in inhibiting HIV infection, curtailing the pool of dNTPs available for reverse transcription of the viral genome. Recent structural data suggested a compelling mechanism for the regulation of SAMHD1 enzymatic activity and revealed dGTP-induced association of two inactive dimers into an active tetrameric enzyme....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Regulation
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Deoxyguanine Nucleotides

Share to Deoxyribonucleotides

Share to Monomeric GTP-Binding Proteins

Share to Nucleic Acid Conformation

Share to Protein Multimerization

Share to SAM Domain and HD Domain-Containing Protein 1

Source

Open in PubMed Open full text

Identifiers

PMID: 25288794
DOI: 10.1074/jbc.M114.591958
PMCID: PMC4239615

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.PMID 25288794Read ↗

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

Uncovering allostery and regulation in SAMHD1 through molecular dynamics simulations.Semantic proximity Read ↗

Tetramerization of SAMHD1 Is Required for Biological Activity and Inhibition of HIV InfectionSemantic proximity Read ↗

SAMHD1 Has Differential Impact on the Efficacies of HIV Nucleoside Reverse Transcriptase InhibitorsSemantic proximity Read ↗

Involvement of SAMHD1 in dNTP homeostasis and the maintenance of genomic integrity and oncotherapy (Review).Semantic proximity Read ↗

Crystal structures of SAMHD1 inhibitor complexes reveal the mechanism of water-mediated dNTP hydrolysis.Semantic proximity Read ↗

Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification.Semantic proximity Read ↗

SAMHD1 Functions and Human Diseases.Semantic proximity Read ↗

The deoxynucleotide triphosphohydrolase SAMHD1 is a major regulator of DNA precursor pools in mammalian cellsSemantic proximity Read ↗

With me or against me: Tumor suppressor and drug resistance activities of SAMHD1.Semantic proximity Read ↗

SAMHD1 acetylation enhances its deoxynucleotide triphosphohydrolase activity and promotes cancer cell proliferationSemantic proximity Read ↗

The ribonuclease activity of SAMHD1 is required for HIV-1 restriction.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.