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

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 l...

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Detalles Bibliográficos
Autores principales: Lee, Chien-Yun, Lin, Chu-Cheng, Liu, Yi-Liang, Liu, Guang-Yaw, Liu, Jyung-Hurng, Hung, Hui-Chih
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5314407/
https://www.ncbi.nlm.nih.gov/pubmed/28209966
http://dx.doi.org/10.1038/srep42662

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5314407/
https://www.ncbi.nlm.nih.gov/pubmed/28209966
http://dx.doi.org/10.1038/srep42662

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