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Specificity and affinity of the N-terminal residues in staphylocoagulase in binding to prothrombin

In Staphylococcus aureus–caused endocarditis, the pathogen secretes staphylocoagulase (SC), thereby activating human prothrombin (ProT) and evading immune clearance. A previous structural comparison of the SC(1–325) fragment bound to thrombin and its inactive precursor prethrombin 2 has indicated th...

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Dettagli Bibliografici
Pubblicato in:J Biol Chem
Autori principali: Maddur, Ashoka A., Kroh, Heather K., Aschenbrenner, Mary E., Gibson, Breanne H. Y., Panizzi, Peter, Sheehan, Jonathan H., Meiler, Jens, Bock, Paul E., Verhamme, Ingrid M.
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Biochemistry and Molecular Biology 2020
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC7186164/
https://ncbi.nlm.nih.gov/pubmed/32156702
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA120.012588
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