Structure of granzyme C reveals an unusual mechanism of protease autoinhibition

Proteases act in important homeostatic pathways and are tightly regulated. Here, we report an unusual structural mechanism of regulation observed by the 2.5-Å X-ray crystal structure of the serine protease, granzyme C. Although the active-site triad residues adopt canonical conformations, the oxyani...

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Bibliografiska uppgifter
Huvudupphovsmän: Kaiserman, Dion, Buckle, Ashley M., Van Damme, Petra, Irving, James A., Law, Ruby H. P., Matthews, Antony Y., Bashtannyk-Puhalovich, Tanya, Langendorf, Chris, Thompson, Philip, Vandekerckhove, Joël, Gevaert, Kris, Whisstock, James C., Bird, Phillip I.
Materialtyp: Artigo
Språk:Inglês
Publicerad: National Academy of Sciences 2009
Ämnen:
Biological Sciences
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC2666993/
https://ncbi.nlm.nih.gov/pubmed/19299505
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0811968106
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