ArticleProtein science : a publication of the Protein Society2021
Structure of Aedes aegypti carboxypeptidase B1-inhibitor complex uncover the disparity between mosquito and non-mosquito insect carboxypeptidase inhibition mechanism.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Comparative molecular dynamics mapping of metallocarboxypeptidase-peptide interfaces reveals potential hotspots that inspire novel inhibitor design.Scientific reports · 2026Article
- Inhibition of carboxypeptidase b1 from Anopheles stephensi by the potato carboxypeptidase inhibitor: a foundational step toward paratransgenesis-based malaria control.Malaria journal · 2026Article
- Molecular Characterization, Recombinant Expression, and Functional Analysis of Carboxypeptidase B inGenes · 2025Article
- The Sexual Dimorphism in Rectum and Protein Digestion Pathway Influence Sex Pheromone Synthesis in Male Bactrocera Dorsalis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Carboxypeptidase inhibitors fromFrontiers in molecular biosciences · 2023Article
- 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
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Authors and funding
6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Metallocarboxypeptidases (MCPs) in the mosquito midgut play crucial roles in infection, as well as in mosquito dietary digestion, reproduction, and development. MCPs are also part of the digestive system of plant-feeding insects, representing key targets for inhibitor development against mosquitoes/mosquito-borne pathogens or as antifeedant molecules against plant-feeding insects. Notably, some non-mosquito insect B-type MCPs are primarily insensitive to plant protease inhibitors (PPIs) such as the potato carboxypeptidase inhibitor (PCI; MW 4 kDa), an inhibitor explored for cancer treatment and insecticide design. Here, we report the crystal structure of Aedes aegypti carboxypeptidase-B1 (CPBAe1)-PCI complex and compared the binding with that of PCI-insensitive CPBs. We show that PCI accommodation is determined by key differences in the active-site regions of MCPs. In particular, the loop regions α6-α7 (Leu
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