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

Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T.

The Journal of biological chemistry - 2 Feb 2007

Stenmark Pål, Kursula Petri, Flodin Susanne, Gräslund Susanne, Landry Robert, Nordlund Pär, Schüler Herwig

Abstract excerpt

Inosine triphosphatase (ITPA) is a ubiquitous key regulator of cellular non-canonical nucleotide levels. It breaks down inosine and xanthine nucleotides generated by deamination of purine bases. Its enzymatic action prevents accumulation of ITP and reduces the risk of incorporation of potentially mutagenic inosine nucleotides into nucleic acids. Here we describe the crystal structure of human ITPA in complex with...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Crystallization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to DNA, Complementary

Share to Protein Conformation

Share to Protein Structure, Secondary

Share to Pyrophosphatases

Share to Recombinant Proteins

Source

Identifiers

PMID: 17138556
DOI: 10.1074/jbc.M609838200

Genes

ITPA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T.PMID 17138556Read ↗

The human ITPA polymorphic variant P32T is destabilized by the unpacking of the hydrophobic core.Semantic proximity Read ↗

Inosine Triphosphate Pyrophosphatase (ITPase): Functions, Mutations, Polymorphisms and Its Impact on Cancer Therapies.Semantic proximity Read ↗

Structural dynamics of inosine triphosphate pyrophosphatase (ITPA) protein and two clinically relevant mutants: molecular dynamics simulations.Semantic proximity Read ↗

Pharmacogenetic significance of inosine triphosphatase.Semantic proximity Read ↗

A disease spectrum for ITPA variation: advances in biochemical and clinical research.Semantic proximity Read ↗

Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms.Semantic proximity Read ↗

Insights into xanthine riboswitch structure and metal ion-mediated ligand recognition.Semantic proximity Read ↗

Characterization of the inosine triphosphatase (ITPA) gene: haplotype structure, haplotype-phenotype correlation and promoter function.Semantic proximity Read ↗

An ITPA Enzyme with Improved Substrate Selectivity.Semantic proximity Read ↗

Quantitative in vitro and in vivo characterization of the human P32T mutant ITPase.Semantic proximity Read ↗

Dual functional roles of ATP in the human mitochondrial malic enzyme.Semantic proximity Read ↗

Protein-protein interfaces as druggable targets: A common motif of the pyridoxal-5’-phosphate-dependent enzymes to receive the coenzyme from its producersSemantic proximity Read ↗

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