ArticleBiophysical journal2010
NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimetics.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras.Frontiers in molecular biosciences · 2022Article
- Structure of Fungal α Mating Pheromone in Membrane Mimetics Suggests a Possible Role for Regulation at the Water-Membrane Interface.Frontiers in microbiology · 2020Article
- Insight into the Antifungal Mechanism of Action of Human RNase N-terminus Derived Peptides.International journal of molecular sciences · 2019Article
- Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans.MicrobiologyOpen · 2016Article
- Basic amino acid residues of human eosinophil derived neurotoxin essential for glycosaminoglycan binding.International journal of molecular sciences · 2013Article
- Two human host defense ribonucleases against mycobacteria, the eosinophil cationic protein (RNase 3) and RNase 7.Antimicrobial agents and chemotherapy · 2013Article
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- In silico prediction and in vitro characterization of multifunctional human RNase3.BioMed research international · 2013Article
- Antimicrobial action and cell agglutination by the eosinophil cationic protein are modulated by the cell wall lipopolysaccharide structure.Antimicrobial agents and chemotherapy · 2012Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eosinophil cationic protein (ECP) is a highly stable, cytotoxic ribonuclease with the ability to enter and disrupt membranes that participates in innate immune defense against parasites but also kills human cells. We have used NMR spectroscopy to characterize the binding of ECP to membrane and heparin mimetics at a residue level. We believe we have identified three Arg-rich surface loops and Trp(35) as crucial for membrane binding. Importantly, we have provided evidence that the interaction surface of ECP with heparin mimetics is extended with respect to that previously described (fragment 34-38). We believe we have identified new sites involved in the interaction for the first time, and shown that the N-terminal alpha-helix, the third loop, and the first and last beta-strands are key for heparin binding. We have also shown that a biologically active ECP N-terminal fragment comprising the first 45 residues (ECP1-45) retains the capacity to bind membrane and heparin mimetics, thus neither the ECP tertiary structure nor its high conformational stability are required for cytotoxicity.
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Registered trials
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.