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TitleGlycosaminoglycans activate peptidylarginine deiminase 4 by enhancing calcium affinity.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 44, Page e2508369122, Year 2025
Publish dateNov 4, 2025
AuthorsGrzegorz P Bereta / Ewa Bielecka / Karolina Marzec / Łukasz Pijanowski / Artur P Biela / Piotr Wilk / Marta Kamińska / Jakub Nowak / Elżbieta Wątor-Wilk / Przemysław Grudnik / Dominik Kowalczyk / Joanna Kozieł / Piotr Mydel / Marcin Poręba / Tomasz Kantyka /
PubMed AbstractRheumatoid arthritis is a chronic inflammatory disease driven by abnormal protein modifications. These include citrullination of arginine residues by the calcium-activated enzyme peptidylarginine ...Rheumatoid arthritis is a chronic inflammatory disease driven by abnormal protein modifications. These include citrullination of arginine residues by the calcium-activated enzyme peptidylarginine deiminase 4 (PAD4). However, calcium in body fluids may not fully activate PAD4, suggesting the potential involvement of other activators. In this study, we investigated the ability of glycosaminoglycans (a class of negatively charged polysaccharides) to modulate PAD4 activity. We found that model glycosaminoglycans bind to the enzyme with a nanomolar affinity, increase its calcium sensitivity, and require enzyme dimerization for activation. These effects depend on the size and negative charge of the glycosaminoglycan, and its various natural forms activate PAD4. Thus, our findings elucidate a mechanism by which common physiological compounds modulate PAD4 activity, potentially contributing to disease etiology.
External linksProc Natl Acad Sci U S A / PubMed:41166417 / PubMed Central
MethodsEM (single particle)
Resolution2.96 - 3.73 Å
Structure data

EMDB-52412: CryoEM structure of human peptidylarginine deiminase type 4 (PAD4) in complex with heparin oligomer (20 subunits) in 0.1 mM calcium
Method: EM (single particle) / Resolution: 3.2 Å

52413

9huh

EMDB-52413, PDB-9huh:
CryoEM structure of human peptidylarginine deiminase type 4 (PAD4) in 10 mM calcium
Method: EM (single particle) / Resolution: 2.96 Å

52414

9hui

EMDB-52414, PDB-9hui:
CryoEM structure of human peptidylarginine deiminase type 4 (PAD4) in complex with heparin oligomer (20 subunits).
Method: EM (single particle) / Resolution: 3.73 Å

52415

9huj

EMDB-52415, PDB-9huj:
CryoEM structure of human peptidylarginine deiminase type 4 (PAD4) in complex with heparin oligomer (12 subunits)
Method: EM (single particle) / Resolution: 3.57 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / PAD4 / citrullination / calcium

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