ArticleJournal of molecular recognition : JMR2018
Electrostatic recognition in substrate binding to serine proteases.
Article in Journal of molecular recognition : JMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Prothrombinase processivity is conferred by substrate allostery.The EMBO journal · 2026Article
- Lactoferrin impairs pathogen virulence through its proteolytic activity.Frontiers in veterinary science · 2024Review
- PEP-Patch: Electrostatics in Protein-Protein Recognition, Specificity, and Antibody Developability.Journal of chemical information and modeling · 2023Article
- Binding modes of prothrombin cleavage site sequences to the factor Xa catalytic triad: Insights from atomistic simulations.Computational and structural biotechnology journal · 2022Article
- Investigation on substrate specificity and catalytic activity of serine protease neuropsin.Biophysics and physicobiology · 2022Article
- Recombinant Production and Characterization of an Extracellular Subtilisin-Like Serine Protease from Acinetobacter baumannii of Fermented Food Origin.The protein journal · 2021Article
- Polyanions Cause Protein Destabilization Similar to That in Live Cells.Biochemistry · 2021Article
- Protein-Protein Binding as a Two-Step Mechanism: Preselection of Encounter Poses during the Binding of BPTI and Trypsin.Biophysical journal · 2020Article
- Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design.Computational and structural biotechnology journal · 2020Review
- Solvation Free Energy as a Measure of Hydrophobicity: Application to Serine Protease Binding Interfaces.Journal of chemical theory and computation · 2019Article
- Electrostatic recognition in substrate binding to serine proteases.Journal of molecular recognition : JMR · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Serine proteases of the Chymotrypsin family are structurally very similar but have very different substrate preferences. This study investigates a set of 9 different proteases of this family comprising proteases that prefer substrates containing positively charged amino acids, negatively charged amino acids, and uncharged amino acids with varying degree of specificity. Here, we show that differences in electrostatic substrate preferences can be predicted reliably by electrostatic molecular interaction fields employing customized GRID probes. Thus, we are able to directly link protease structures to their electrostatic substrate preferences. Additionally, we present a new metric that measures similarities in substrate preferences focusing only on electrostatics. It efficiently compares these electrostatic substrate preferences between different proteases. This new metric can be interpreted as the electrostatic part of our previously developed substrate similarity metric. Consequently, we suggest, that substrate recognition in terms of electrostatics and shape complementarity are rather orthogonal aspects of substrate recognition. This is in line with a 2-step mechanism of protein-protein recognition suggested in the literature.
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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.