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Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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...
Integrins01:10

Integrins

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,...
Activation of Integrins01:15

Activation of Integrins

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 events provide an effective stimulus.
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...

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A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
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α(V)β(3) integrin crystal structures and their functional implications.

Xianchi Dong1, Li-Zhi Mi, Jianghai Zhu

  • 1Immune Disease Institute, Children's Hospital Boston, and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 3 Blackfan Circle, Boston, Massachusetts 02115, United States.

Biochemistry
|October 31, 2012
PubMed
Summary
This summary is machine-generated.

Structural studies of integrin α(V)β(3) reveal flexibility between extracellular and transmembrane domains, challenging previous models of rigid linkage and supporting large conformational changes for activation.

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Area of Science:

  • Structural biology
  • Biochemistry
  • Cellular signaling

Background:

  • Integrins are crucial cell surface receptors involved in cell adhesion and signaling.
  • The activation mechanism of integrin α(V)β(3) remains incompletely understood, particularly the role of its structural features.

Purpose of the Study:

  • To determine and refine crystal structures of integrin α(V)β(3) ectodomains with varying transmembrane linker lengths.
  • To investigate the structural basis of integrin α(V)β(3) activation and ligand binding.

Main Methods:

  • X-ray crystallography of integrin α(V)β(3) ectodomains linked to coiled coils (α(V)β(3)-AB) and transmembrane domains (α(V)β(3)-1TM).
  • Structure re-refinement and analysis of electron density.

Main Results:

  • Crystal structures reveal bent ectodomains in a closed, low-affinity conformation.
  • Metal-binding site occupancy is pH-dependent, not directly linked to physiological regulation.
  • Observed flexibility in the linker between extracellular and transmembrane domains, contradicting rigid linkage models.
  • No evidence for a previously proposed interface between α(V) and β(3) subunits at their knees.

Conclusions:

  • Integrin α(V)β(3) exhibits flexibility in its linker region, suggesting large conformational changes are necessary for activation.
  • Findings support a model where extracellular domain extension and headpiece opening transmit activation signals.