Structural insight into the function of human peptidyl arginine deiminase 6.
Citrullination
Infertility
Peptidyl arginine deiminase
Protein folding
Protein mutation damage prediction
X-Ray crystallography
Journal
Computational and structural biotechnology journal
ISSN: 2001-0370
Titre abrégé: Comput Struct Biotechnol J
Pays: Netherlands
ID NLM: 101585369
Informations de publication
Date de publication:
Dec 2024
Dec 2024
Historique:
received:
14
06
2024
revised:
15
08
2024
accepted:
15
08
2024
medline:
17
9
2024
pubmed:
17
9
2024
entrez:
17
9
2024
Statut:
epublish
Résumé
Peptidyl arginine deiminase 6 (PADI6 or PAD6) is vital for early embryonic development in mice and humans, yet its function remains elusive. PADI6 is less conserved than other PADIs and it is currently unknown whether it has a catalytic function. Here we show that human PADI6 dimerises like hPADIs 2-4, however, does not bind Ca
Identifiants
pubmed: 39286527
doi: 10.1016/j.csbj.2024.08.019
pii: S2001-0370(24)00278-2
pmc: PMC11402830
doi:
Types de publication
Journal Article
Langues
eng
Pagination
3258-3269Informations de copyright
© 2024 The Authors.
Déclaration de conflit d'intérêts
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.