ArticleThe FEBS journal2014
Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme.
Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Metabolites Isolated fromInternational journal of molecular sciences · 2025Article
- Molecular Basis of Dipeptide Recognition inBiomolecules · 2025Article
- Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.ACS pharmacology & translational science · 2022Review
- The Drosophila melanogaster ACE2 ortholog genes are differently expressed in obesity/diabetes and aging models: Implications for COVID-19 pathology.Biochimica et biophysica acta. Molecular basis of disease · 2022Article
- Cryo-EM reveals mechanisms of angiotensin I-converting enzyme allostery and dimerization.The EMBO journal · 2022Article
- Conformational Variation in Enzyme Catalysis: A Structural Study on Catalytic Residues.Journal of molecular biology · 2022Article
- Structure ofLife science alliance · 2022Article
- Small molecule angiotensin converting enzyme inhibitors: A medicinal chemistry perspective.Frontiers in pharmacology · 2022Review
- Structure of Aedes aegypti carboxypeptidase B1-inhibitor complex uncover the disparity between mosquito and non-mosquito insect carboxypeptidase inhibition mechanism.Protein science : a publication of the Protein Society · 2021Article
- ACE and ACE2: insights fromHeliyon · 2021Review
- ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV.Clinical science (London, England : 1979) · 2020Review
- Novel Therapeutic Approaches Targeting the Renin-Angiotensin System and Associated Peptides in Hypertension and Heart Failure.Pharmacological reviews · 2019Review
- Targeting Metalloenzymes for Therapeutic Intervention.Chemical reviews · 2019Review
- Discovery of Anti-Hypertensive Oligopeptides from Adlay Based on In Silico Proteolysis and Virtual Screening.International journal of molecular sciences · 2016Article
- Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme.Scientific reports · 2015Article
- A new high-resolution crystal structure of the Drosophila melanogaster angiotensin converting enzyme homologue, AnCE.FEBS open bio · 2015Article
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
Human somatic angiotensin-I converting enzyme (ACE) is a zinc-dependent dipeptidyl carboxypeptidase and a central component of the renin angiotensin aldosterone system (RAAS). Its involvement in the modulation of physiological actions of peptide hormones has positioned ACE as an important therapeutic target for the treatment of hypertension and cardiovascular disorders. Here, we report the crystal structures of the two catalytic domains of human ACE (N- and C-) in complex with FI, the S enantiomer of the phosphinic ACE/ECE-1 (endothelin converting enzyme) dual inhibitor FII, to a resolution of 1.91 and 1.85 Å, respectively. In addition, we have determined the structure of AnCE (an ACE homologue from Drosophila melanogaster) in complex with both isomers. The inhibitor FI (S configuration) can adapt to the active site of ACE catalytic domains and shows key differences in its binding mechanism mostly through the reorientation of the isoxazole phenyl side group at the P₁' position compared with FII (R configuration). Differences in binding are also observed between FI and FII in complex with AnCE. Thus, the new structures of the ACE-inhibitor complexes presented here provide useful information for further exploration of ACE inhibitor pharmacophores involving phosphinic peptides and illustrate the role of chirality in enhancing drug specificity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.