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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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| Gepubliceerd in: | Sci Rep |
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| Hoofdauteurs: | , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Nature Publishing Group
2017
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5314407/ https://ncbi.nlm.nih.gov/pubmed/28209966 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/srep42662 |
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