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

Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies.

Journal of molecular biology - 6 Jun 2008

Zha Manwu, Guo Qing, Zhang Yichun, Yu Biao, Ou Ying, Zhong Chen, Ding Jianping

Abstract excerpt

Human NUDT5 (hNUDT5) is an ADP-ribose (ADPR) pyrophosphatase (ADPRase) that plays important roles in controlling the intracellular levels of ADPR and preventing non-enzymatic ADP-ribosylation of proteins by hydrolyzing ADPR to AMP and ribose 5'-phosphate. We report the crystal structure of hNUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg(2+) ions...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate Ribose
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Magnesium

Share to Molecular Structure

Share to Protein Structure, Quaternary

Share to Pyrophosphatases

Share to Sequence Alignment

Source

Identifiers

PMID: 18462755
DOI: 10.1016/j.jmb.2008.04.006

Genes

NUDT5

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies.PMID 18462755Read ↗

Analysis of ligand binding and resulting conformational changes in pyrophosphatase NUDT9.Semantic proximity Read ↗

Crystal and EM structures of human phosphoribosyl pyrophosphate synthase I (PRS1) provide novel insights into the disease-associated mutations.Semantic proximity Read ↗

Role of NUDIX Hydrolases in NAD and ADP-Ribose Metabolism in MammalsSemantic proximity Read ↗

[Mechanistic insight into hydrolysis of oxidized nucleotide diphosphates by human NUDT5].Semantic proximity Read ↗

Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal.Semantic proximity Read ↗

Kinetic and mutational studies of the adenosine diphosphate ribose hydrolase from Mycobacterium tuberculosis.Semantic proximity Read ↗

NUDT5 regulates purine metabolism and thiopurine sensitivity by interacting with PPATSemantic proximity Read ↗

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

Structure-function relationships of the ADP/ATP carrier.Semantic proximity Read ↗

Modelling dynamics of human NDPK hexamer structure, stability and interactionsSemantic proximity Read ↗

Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.Semantic proximity Read ↗

ADP-ribosylation from molecular mechanisms to therapeutic implicationsSemantic proximity Read ↗

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