Ontology highlight
ABSTRACT:
SUBMITTER: Luo Y
PROVIDER: S-EPMC1808342 | biostudies-literature | 2006 Oct
REPOSITORIES: biostudies-literature
Luo Yuan Y Arita Kyouhei K Bhatia Monica M Knuckley Bryan B Lee Young-Ho YH Stallcup Michael R MR Sato Mamoru M Thompson Paul R PR
Biochemistry 20061001 39
Protein arginine deiminase 4 (PAD4) is a transcriptional coregulator that catalyzes the calcium-dependent conversion of specific arginine residues in proteins to citrulline. Recently, we reported the synthesis and characterization of F-amidine, a potent and bioavailable irreversible inactivator of PAD4. Herein, we report our efforts to identify the steric and leaving group requirements for F-amidine-induced PAD4 inactivation, the structure of the PAD4-F-amidine x calcium complex, and in vivo stu ...[more]