Frontiers in Molecular Biosciences is pleased to present 'Allosteric Functions and Inhibitions: Structural Insights', as part of the 'Allosteric Functions and Inhibitions' mini-series.
Allostery, also known as “action at a distance”, is essential for biological regulation, including examples in gene regulation and enzymatic pathways. Here, interaction with a small molecule ligand and/or a macromolecular binding partner, mutation or covalent modification results in remote effects, including changes to protein structure, dynamics and function. Allosteric regulation has broad implications in biotechnology, synthetic biology and medicine. Allosteric sites, conventional and cryptic, offer novel drug interaction sites for therapeutic interventions. There is also great interest in engineering and modifying allosteric regulation in proteins for a variety of purposes, including in the production of biofuels and other high value commodities.
Allostery in a variety of protein systems continues to be highly investigated. Classical models of allostery, including the concerted Monod-Wyman-Changeux (MWC) and sequential Koshland-Nemethy-Filmer (KNF) models, have given rise to more encompassing models, including those based on protein conformational ensembles. These advances have been made possible through improvements in structural techniques, including X-ray crystallography, NMR, cryo-electron microscopy and mass spectrometry, as well as complementary advances in other biophysical and chemical methods. We wish to highlight how structural and related experimental methods have contributed to our understanding of allostery, especially how new atomic-level insights broaden and leverage our understanding of allosteric mechanisms.
The aim of the current Research Topic is to cover promising, recent, and novel research trends in allosteric regulation. Areas to be covered in this Research Topic may include, but are not limited to:
• Advances in structure-driven methods investigating allostery, highlighting developments in methodology and data interpretation.
• Integrative studies including those that combine structural insights with complementary biophysical, chemical and computational methods.
• Structure-based insights into models and mechanisms of allostery, including ensemble, dynamic and network views of allostery.
We are interested in receiving a variety of Article types including Original Research, Methods, Hypothesis and Theory, Perspective, Opinion and Review.
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Prof. Emily Parker is a founder of private company Bontia Bio, and is in partnership with the following companies: Biotelliga, EBOSS, Merck, Elanco, Dow Agri-sciences, Argenta, South Pacific Sera, and NZ Pharmaceuticals.
Frontiers in Molecular Biosciences is pleased to present 'Allosteric Functions and Inhibitions: Structural Insights', as part of the 'Allosteric Functions and Inhibitions' mini-series.
Allostery, also known as “action at a distance”, is essential for biological regulation, including examples in gene regulation and enzymatic pathways. Here, interaction with a small molecule ligand and/or a macromolecular binding partner, mutation or covalent modification results in remote effects, including changes to protein structure, dynamics and function. Allosteric regulation has broad implications in biotechnology, synthetic biology and medicine. Allosteric sites, conventional and cryptic, offer novel drug interaction sites for therapeutic interventions. There is also great interest in engineering and modifying allosteric regulation in proteins for a variety of purposes, including in the production of biofuels and other high value commodities.
Allostery in a variety of protein systems continues to be highly investigated. Classical models of allostery, including the concerted Monod-Wyman-Changeux (MWC) and sequential Koshland-Nemethy-Filmer (KNF) models, have given rise to more encompassing models, including those based on protein conformational ensembles. These advances have been made possible through improvements in structural techniques, including X-ray crystallography, NMR, cryo-electron microscopy and mass spectrometry, as well as complementary advances in other biophysical and chemical methods. We wish to highlight how structural and related experimental methods have contributed to our understanding of allostery, especially how new atomic-level insights broaden and leverage our understanding of allosteric mechanisms.
The aim of the current Research Topic is to cover promising, recent, and novel research trends in allosteric regulation. Areas to be covered in this Research Topic may include, but are not limited to:
• Advances in structure-driven methods investigating allostery, highlighting developments in methodology and data interpretation.
• Integrative studies including those that combine structural insights with complementary biophysical, chemical and computational methods.
• Structure-based insights into models and mechanisms of allostery, including ensemble, dynamic and network views of allostery.
We are interested in receiving a variety of Article types including Original Research, Methods, Hypothesis and Theory, Perspective, Opinion and Review.
----------
Prof. Emily Parker is a founder of private company Bontia Bio, and is in partnership with the following companies: Biotelliga, EBOSS, Merck, Elanco, Dow Agri-sciences, Argenta, South Pacific Sera, and NZ Pharmaceuticals.
