Related Experiment Video
Updated: Oct 31, 2025
12:38
Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
Published on: February 15, 2018
20.2K
Fuzzy binding model of molecular interactions between tropoelastin and integrin alphaVbeta3
Jazmin Ozsvar1, Richard Wang1, Anna Tarakanova2
1Charles Perkins Centre, The University of Sydney, Sydney, Australia; School of Life and Environmental Sciences, The University of Sydney, Sydney, Australia.
Biophysical Journal
|July 1, 2021
Summary
Tropoelastin, the building block of elastin, interacts with integrin αvβ3 through a flexible "fuzzy binding" mechanism. This process involves multiple tropoelastin sites and integrin regions, crucial for tissue resilience.
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- Elastin provides resilience to extracellular matrix in elastic tissues.
- Tropoelastin is the monomeric precursor to elastin.
- Integrin-mediated cell signaling is vital for tissue function.
Purpose of the Study:
- To model the molecular interactions between tropoelastin and integrin αvβ3.
- To elucidate the mechanism of tropoelastin binding to integrins.
- To understand the role of flexible protein interactions in biological signaling.
Main Methods:
- Full atomistic molecular modeling.
- Ensemble-based computational methodologies.
- Analysis of protein-protein interactions.
Main Results:
- Tropoelastin binding to integrin αvβ3 occurs via a "fuzzy binding" model.
- Multiple tropoelastin conformations and integrin regions cooperatively interact.
- Binding to the α1 helix facilitates integrin conformational changes more than the canonical site.
Conclusions:
- The fuzzy binding model explains experimental observations of tropoelastin-integrin interactions.
- Ensemble-based approaches are effective for studying flexible protein mechanisms.
- Understanding these interactions is key to extracellular matrix resilience and signaling.
Related Concept Videos
01:17Intracellular Signaling Affects Focal Adhesions
3.1K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
3.1K
01:15Activation of Integrins
4.2K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
4.2K
01:10Integrins
4.6K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
4.6K
01:12Elastin is Responsible for Tissue Elasticity
2.7K
Elastic fiber contains the protein elastin along with lesser amounts of other proteins and glycoproteins. The main property of elastin is that it will return to its original shape after being stretched or compressed. Elastic fibers are prominent in elastic tissues found in skin and the elastic ligaments of the vertebral column.
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...
Ligaments and tendons are made of dense regular connective tissue, but in ligaments not all fibers are parallel. Dense regular elastic tissue contains elastin fibers and...
2.7K
01:58Cooperative Allosteric Transitions
8.3K
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...
8.3K
01:24Overview of Cell-Matrix Interactions
8.2K
The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
8.2K