Related Experiment Video
Updated: Jul 19, 2025
10:59
Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
Published on: August 17, 2022
3.2K
Effector-dependent structural transformation of a crystalline framework with allosteric effects on molecular
Ryunosuke Hayashi1, Shohei Tashiro2, Masahiro Asakura1
1Department of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Nature Communications
|August 10, 2023
Summary
Flexible porous crystals exhibit allosteric control, where effector binding triggers structural changes. This stimuli-responsive behavior in ordered materials offers new avenues for designing advanced functional materials for biological applications.
Area of Science:
- Materials Science
- Supramolecular Chemistry
- Biomimetic Materials
Background:
- Structurally flexible porous crystals with high regularity and stimuli responsiveness are inspired by allosteric regulation in biological systems.
- Porous crystals featuring molecular recognition sites are key for functional control via effector-induced structural distortion.
Purpose of the Study:
- To demonstrate allosteric control over porous molecular crystal structure via local effector adsorption.
- To investigate effector-dependent framework structural conversion and switching of molecular affinity.
Main Methods:
- Utilized low-symmetry nanochannels with multiple molecular recognition sites within porous crystals.
- Investigated the adsorption of effectors and their impact on crystal structure and molecular recognition properties.
Main Results:
- Achieved allosteric control of porous crystal structure through local effector adsorption.
- Demonstrated effector-dependent structural conversion and tunable molecular affinity at recognition sites.
- Showcased stimuli-responsive, adaptable framework behavior.
Conclusions:
- Porous molecular crystals can be allosterically controlled by local effector adsorption.
- This approach enables effector-dependent structural conversion and modulation of molecular recognition.
- Provides a framework for developing advanced supramolecular materials for biological applications.
Related Concept Videos
01:58Cooperative Allosteric Transitions
7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
01:08Allosteric Regulation
58.2K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
58.2K
01:19Allosteric Proteins-ATCase
5.8K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.8K
00:49Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K
01:27Transducer Mechanism: Enzyme-Linked Receptors
2.5K
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Major types that are helpful drug targets include:
2.5K
01:00Enzyme-linked Receptors
78.7K
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
78.7K