Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment

Bacterial α-2-macroglobulins have been suggested to function in defence as broad-spectrum inhibitors of host proteases that breach the outer membrane. Here, the X-ray structure of protease-cleaved Escherichia coli α-2-macroglobulin is described, which reveals a putative mechanism of activation and c...

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Vydáno v:Acta Crystallogr D Biol Crystallogr
Hlavní autoři: Fyfe, Cameron D., Grinter, Rhys, Josts, Inokentijs, Mosbahi, Khedidja, Roszak, Aleksander W., Cogdell, Richard J., Wall, Daniel M., Burchmore, Richard J. S., Byron, Olwyn, Walker, Daniel
Médium: Artigo
Jazyk:Inglês
Vydáno: International Union of Crystallography 2015
Témata:
Research Papers
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC4498604/
https://ncbi.nlm.nih.gov/pubmed/26143919
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1399004715008548
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