Cargando…
ACE-domain selectivity extends beyond direct interacting residues at the active site
Angiotensin-converting enzyme (ACE) is best known for its formation of the vasopressor angiotensin II that controls blood pressure but is also involved in other physiological functions through the hydrolysis of a variety of peptide substrates. The enzyme contains two catalytic domains (nACE and cACE...
Autores principales: | Cozier, Gyles E., Lubbe, Lizelle, Sturrock, Edward D., Acharya, K. Ravi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7148434/ https://www.ncbi.nlm.nih.gov/pubmed/32195541 http://dx.doi.org/10.1042/BCJ20200060 |
Ejemplares similares
-
ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV
por: Lubbe, Lizelle, et al.
Publicado: (2020) -
Angiotensin‐converting enzyme open for business: structural insights into the subdomain dynamics
por: Cozier, Gyles E., et al.
Publicado: (2020) -
Crystal structures of sampatrilat and sampatrilat‐Asp in complex with human ACE – a molecular basis for domain selectivity
por: Cozier, Gyles E., et al.
Publicado: (2018) -
Molecular Basis
for Omapatrilat and Sampatrilat Binding
to Neprilysin—Implications for Dual Inhibitor Design with Angiotensin-Converting
Enzyme
por: Sharma, Urvashi, et al.
Publicado: (2020) -
Fragment-based design for the development of N-domain-selective angiotensin-1-converting enzyme inhibitors
por: Douglas, Ross G., et al.
Publicado: (2013)