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 for Ca(2+)-induced activation of human PAD4.

Nature structural & molecular biology - 1 Aug 2004

Arita Kyouhei, Hashimoto Hiroshi, Shimizu Toshiyuki, Nakashima Katsuhiko, Yamada Michiyuki, Sato Mamoru

Abstract excerpt

Peptidylarginine deiminase 4 (PAD4) is a Ca(2+)-dependent enzyme that catalyzes the conversion of protein arginine residues to citrulline. Its gene is a susceptibility locus for rheumatoid arthritis. Here we present the crystal structure of Ca(2+)-free wild-type PAD4, which shows that the polypeptide chain adopts an elongated fold in which the N-terminal domain forms two immunoglobulin-like subdomains, and the...

Read the complete abstract on PubMed

Topics

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

Share to Cadmium
Share to Citrulline
Share to Hydrolases

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

Share to Hydrolysis

Share to Models, Chemical

Share to Protein-Arginine Deiminase Type 4

Share to Protein-Arginine Deiminases

Source

Identifiers

PMID: 15247907
DOI: 10.1038/nsmb799

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for Ca(2+)-induced activation of human PAD4.PMID 15247907Read ↗

Probing the Roles of Calcium-Binding Sites during the Folding of Human Peptidylarginine Deiminase 4.Semantic proximity Read ↗

Peptidylarginine deiminase 4 and citrullination in health and disease.Semantic proximity Read ↗

Functional roles of the non-catalytic calcium-binding sites in the N-terminal domain of human peptidylarginine deiminase 4.Semantic proximity Read ↗

PAD4: pathophysiology, current therapeutics and future perspective in rheumatoid arthritisSemantic proximity Read ↗

Structural and biochemical analyses of the human PAD4 variant encoded by a functional haplotype gene.Semantic proximity Read ↗

Autocitrullination of human peptidyl arginine deiminase type 4 regulates protein citrullination during cell activationSemantic proximity Read ↗

Structural Insight into the Function of Human Peptidyl Arginine Deiminase 6Semantic proximity Read ↗

Alleviation of arthritis through prevention of neutrophil extracellular traps by an orally available inhibitor of protein arginine deiminase 4Semantic proximity Read ↗

PAD, a growing family of citrullinating enzymes: genes, features and involvement in diseaseSemantic proximity Read ↗

A common missense variant rs874881 of PADI4 gene and rheumatoid arthritis: Genetic association study and in-silico analysis.Semantic proximity Read ↗

Evolutionary origin, cyclic peptide targeting and physiological activation of Peptidyl Arginine Deiminase 4Semantic proximity Read ↗

Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung DiseaseSemantic proximity Read ↗

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