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Article

Molecular Interplay between the Dimer Interface and the Substrate-Binding Site of Human Peptidylarginine Deiminase 4.

Scientific reports - 17 Feb 2017

Lee Chien-Yun, Lin Chu-Cheng, Liu Yi-Liang, Liu Guang-Yaw, Liu Jyung-Hurng, Hung Hui-Chih

Abstract excerpt

Our previous studies suggest that the fully active form of Peptidylarginine deiminase 4 (PAD4) should be a dimer and not a monomer. This paper provides a plausible mechanism for the control of PAD4 catalysis by molecular interplay between its dimer-interface loop (I-loop) and its substrate-binding loop (S-loop). Mutagenesis studies revealed that two hydrophobic residues, W347 and V469, are critical for substrate...

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Identifiers

PMID: 28209966
DOI: 10.1038/srep42662
PMCID: PMC5314407

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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.

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