Exosite binding modulates the specificity of the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease

Autor: Monica Jain, Malgorzata Teçza, Todd F. Kagawa, Jakki C. Cooney

Publikováno v: Computational and Structural Biotechnology Journal, Vol 20, Iss , Pp 4860-4869 (2022)

The C5a peptidase from Streptococcus pyogenes (ScpA) is a highly specific enzyme with potential therapeutic value. ScpA is a good model for studying determinants of specificity in the multidomain immunomodulatory enzymes (IMEs), which comprise a larg

Externí odkaz: https://doaj.org/article/f4c622c71e98439282aac8498091788e

Enzyme kinetic and binding studies identify determinants of specificity for the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease

Autor: Todd F. Kagawa, Malgorzata Teçza, Monica Jain, Jakki C. Cooney

Publikováno v: Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 2356-2365 (2021)

Graphical abstract
The Streptococcal C5a peptidase (ScpA) specifically inactivates the human complement factor hC5a, a potent anaphylatoxin recently identified as a therapeutic target for treatment of COVID-19 infections. Biologics used to modul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a367c25f761a21969cb9ee8b69a1d12f
https://doi.org/10.1016/j.csbj.2021.04.024