Results 21 to 30 of about 18,737 (212)
Communication over the network of binary switches regulates the activation of A$_{2A}$ adenosine receptor [PDF]
, 2014 Dynamics and functions of G-protein coupled receptors (GPCRs) are accurately regulated by the type of ligands that bind to the orthosteric or allosteric binding sites.
Choi, Sun, Hyeon, Changbong, Lee, Yoonji
core +13 more sources
Nature Communications, 2023 Biological regulation ubiquitously depends on protein allostery, but the regulatory mechanisms are incompletely understood, especially in proteins that undergo ligand-induced allostery with few structural changes. Here we used hydrogen-deuterium exchange
Anum Glasgow +5 more
doaj +1 more source
Rigid Residue Scan Simulations Systematically Reveal Residue Entropic Roles in Protein Allostery. [PDF]
PLoS Computational Biology, 2016 Intra-protein information is transmitted over distances via allosteric processes. This ubiquitous protein process allows for protein function changes due to ligand binding events.
Robert Kalescky +3 more
doaj +1 more source
Role of water-bridged interactions in metal ion coupled protein allostery.
PLoS Computational Biology, 2022 Allosteric communication between distant parts of proteins controls many cellular functions, in which metal ions are widely utilized as effectors to trigger the allosteric cascade.
Xingyue Guan +4 more
doaj +1 more source
Allosteric crosstalk in modular proteins: Function fine-tuning and drug design
Computational and Structural Biotechnology Journal, 2023 Modular proteins are regulatory proteins that carry out more than one function. These proteins upregulate or downregulate a biochemical cascade to establish homeostasis in cells.
Suman Abhishek +4 more
doaj +1 more source
Allostery in membrane proteins [PDF]
Current Opinion in Structural Biology, 2020 Membrane proteins are an integral part of signal transduction. To signal, membrane proteins must interact with a variety of lipid species, effectors, and other proteins in the biological membrane leading to an immense number of possible interactions. Despite this inherent complexity, accurate control of signaling must take place.
Cournia, Zoe, Chatzigoulas, Alexios
openaire +3 more sources
Allostery through DNA drives phenotype switching
Nature Communications, 2021 Most insights on DNA-mediated allostery upon transcription factor (TF) binding were either based on artificial promoters or found to be short-ranged. Here authors use single-molecule FRET and cryo-EM to show that Bacillus subtilis bacteria utilize long ...
Gabriel Rosenblum +5 more
doaj +1 more source
Allostery Frustrates the Experimentalist
Journal of Molecular Biology, 2023 Proteins interact with other proteins, with nucleic acids, lipids, carbohydrates and various small molecules in the living cell. These interactions have been quantified and structurally characterized in numerous studies such that we today have a comprehensive picture of protein structure and function.
Gianni, Stefano, Jemth, Per
openaire +3 more sources
The genotype‐phenotype landscape of an allosteric protein
Molecular Systems Biology, 2021 Allostery is a fundamental biophysical mechanism that underlies cellular sensing, signaling, and metabolism. Yet a quantitative understanding of allosteric genotype‐phenotype relationships remains elusive.
Drew S Tack +8 more
doaj +1 more source
Allostery in the dynamic coactivator domain KIX occurs through minor conformational micro-states.
PLoS Computational Biology, 2022 The coactivator KIX of CBP uses two binding surfaces to recognize multiple activators and exhibits allostery in ternary complex formation. Activator•coactivator interactions are central to transcriptional regulation, yet the microscopic origins of ...
Amanda L Peiffer +4 more
doaj +1 more source