Crystal structures of sampatrilat and sampatrilat‐Asp in complex with human ACE – a molecular basis for domain selectivity-Reference-Cited by-同舟云学术

Crystal structures of sampatrilat and sampatrilat‐Asp in complex with human ACE – a molecular basis for domain selectivity

Published:2018-03-08 Issue:8 Volume:285 Page:1477-1490
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Cozier Gyles E.¹,Schwager Sylva L.²,Sharma Rajni K.³,Chibale Kelly³,Sturrock Edward D.²,Acharya K. Ravi¹^ORCID

Affiliation:

1. Department of Biology and Biochemistry University of Bath UK

2. Department of Integrative Biomedical Sciences Institute of Infectious Disease and Molecular Medicine University of Cape Town South Africa

3. South African Medical Research Council Drug Discovery and Development Research Unit Department of Chemistry and Institute of Infectious Disease and Molecular Medicine University of Cape Town South Africa

Funder

Medical Research Council

National Research Foundation

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.14421

Reference41 articles.

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3. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin

4. Peptidase Specificity Characterization of C- and N-Terminal Catalytic Sites of Angiotensin I-Converting Enzyme

5. The Hemoregulatory Peptide N-Acetyl-Ser-Asp-Lys-Pro Is a Natural and Specific Substrate of the N-terminal Active Site of Human Angiotensin-converting Enzyme

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