Discovery of a novel conformational equilibrium in urokinase-type plasminogen activator

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 activator (uP...

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Detalles Bibliográficos
Autores principales: Kromann-Hansen, Tobias, Louise Lange, Eva, Peter Sørensen, Hans, Hassanzadeh-Ghassabeh, Gholamreza, Huang, Mingdong, Jensen, Jan K., Muyldermans, Serge, Declerck, Paul J., Komives, Elizabeth A., Andreasen, Peter A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469797/
https://www.ncbi.nlm.nih.gov/pubmed/28611361
http://dx.doi.org/10.1038/s41598-017-03457-7

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5469797/
https://www.ncbi.nlm.nih.gov/pubmed/28611361
http://dx.doi.org/10.1038/s41598-017-03457-7

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