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Hidden electrostatic basis of dynamic allostery in a PDZ domain
Proceedings of the National Academy of Sciences of the United States of America, 2017 Significance Allosteric regulation is a crucial component in biochemical pathways, where ligand binding to an allosteric site modulates the enzymatic activity at a distant functional site.
Amit Kumawat, Suman Chakrabarty
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Correlating allostery with rigidity
Molecular BioSystems, 2010Abstract Allosteric proteins demonstrate the phenomenon of a ligand binding to a protein at a regulatory or effector site and thereby changing the chemical affinity of the catalytic site. As such, allostery is extremely important biologically as a regulatory mechanism for molecular concentrations in many cellular processes.
A J, Rader, Stephen M, Brown
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Allostery: The Rebound of Proteins
2020The discovery of hemoglobin allosteric properties is briefly summarized and contextualized in the frame of the main biochemical revelations that characterized the first half of the XX century. In particular, the historical background of DNA, RNA, and protein structure research is recalled and the new role that protein-protein interaction may have on ...
Alessandro, Finazzi Agrò +1 more
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A Chemical Perspective on Allostery
Chemical Reviews, 2016Much work has been done in the past decade to quantify the phenomenon of allosteric communication in proteins. Every new study unveils an extra piece of the puzzle in our search for an understanding of allostery that allows us to make predictions on the response of a protein to medically relevant stimuli such as pathological mutations or drug binding ...
Andre A S T, Ribeiro, Vanessa, Ortiz
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Current Opinion in Structural Biology, 2017
Modern interpretations of allostery typically rely on conformational ensembles to describe enzyme function. Conformational motions controlling these ensembles are often stimulated or quenched by allosteric effectors, and are critical to optimizing ligand binding pockets and enzyme architectures.
George P, Lisi, J Patrick, Loria
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Modern interpretations of allostery typically rely on conformational ensembles to describe enzyme function. Conformational motions controlling these ensembles are often stimulated or quenched by allosteric effectors, and are critical to optimizing ligand binding pockets and enzyme architectures.
George P, Lisi, J Patrick, Loria
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Review: Allostery in Chaperonins
Journal of Structural Biology, 2001Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
A, Horovitz +3 more
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Piezoelectric allostery of protein
Physical Review E, 2016Allostery is indispensable for a protein to work, where a locally applied stimulus is transmitted to a distant part of the molecule. While the allostery due to chemical stimuli such as ligand binding has long been studied, the growing interest in mechanobiology prompts the study of the mechanically stimulated allostery, the physical mechanism of which ...
Jun, Ohnuki +2 more
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Journal of Molecular Biology, 2013
The ability to regulate gene expression is essential for controlling metabolic events in a cell. Proteins that function like molecular switches respond to fluctuations in the environment to maintain homeostasis. The operon model, proposed by Jacob and Monod, provides a cogent depiction for how gene expression is regulated. A molecular mechanism for the
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The ability to regulate gene expression is essential for controlling metabolic events in a cell. Proteins that function like molecular switches respond to fluctuations in the environment to maintain homeostasis. The operon model, proposed by Jacob and Monod, provides a cogent depiction for how gene expression is regulated. A molecular mechanism for the
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2019
Allosteric regulation is a ubiquitous strategy employed in nature to control cellular processes by regulating the affinities of biomolecules. Allosteric modulators are able to tune the protein/substrate affinity in a highly predictable way, suggesting that such modulators may represent safe drugs.
Xi, Cheng, Hualiang, Jiang
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Allosteric regulation is a ubiquitous strategy employed in nature to control cellular processes by regulating the affinities of biomolecules. Allosteric modulators are able to tune the protein/substrate affinity in a highly predictable way, suggesting that such modulators may represent safe drugs.
Xi, Cheng, Hualiang, Jiang
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Rendiconti Lincei, 2006
Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
Amnon Horovitz +3 more
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Chaperonins mediate protein folding in an ATP-dependent manner. ATP binding and hydrolysis by chaperonins are subject to both homotropic and heterotropic allosteric regulation. In the case of GroEL and CCT, homotropic regulation by ATP is manifested in nested cooperativity, which involves positive intra-ring cooperativity and negative inter-ring ...
Amnon Horovitz +3 more
openaire +1 more source