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Role of the I16-D194 ionic interaction in the trypsin fold
Activity in trypsin-like proteases is the result of proteolytic cleavage at R15 followed by an ionic interaction that ensues between the new N terminus of I16 and the side chain of the highly conserved D194. This mechanism of activation, first proposed by Huber and Bode, organizes the oxyanion hole...
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| 出版年: | Sci Rep |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group UK
2019
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6889508/ https://ncbi.nlm.nih.gov/pubmed/31792294 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-019-54564-6 |
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