Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator
Abstract Although trypsin-like serine proteases have flexible surface-exposed loops and are known to adopt higher and lower activity conformations, structural determinants for the different conformations have remained largely obscure. The trypsin-like serine protease, urokinase-type plasminogen acti...
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| Auteurs principaux: | , , , , , , , , , |
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| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2017
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| Accès en ligne: | https://doaj.org/article/409897e4334a4c2c81d516f9a73f9d64 |
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