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Related Concept Videos

Metal-Ligand Bonds02:51

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
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.
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...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...

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Updated: Jul 8, 2026

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Published on: May 18, 2009

Integrins, cations and ligands: making the connection.

J-P Xiong1, T Stehle, S L Goodman

  • 1Renal Unit, Leukocyte Biology & Inflammation Program, Structural Biology Program, Massachusetts General Hospital, Charlestown, MA 02129, USA.

Journal of Thrombosis and Haemostasis : JTH
|July 23, 2003
PubMed
Summary
This summary is machine-generated.

Integrins, crucial cell adhesion receptors, mediate bidirectional signaling essential for cell functions. Recent structural studies reveal how cation-dependent changes in integrins control activation, ligand binding, and signaling pathways.

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Last Updated: Jul 8, 2026

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Published on: May 18, 2009

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Integrins are vital cell adhesion receptors mediating cell-extracellular matrix and cell-cell interactions.
  • These receptors link external stimuli to intracellular responses, impacting numerous cellular functions.
  • Understanding integrin structure and cation dependency is key to deciphering cell signaling.

Purpose of the Study:

  • To investigate the structural basis of integrin-mediated bidirectional signaling.
  • To elucidate the role of divalent cations in integrin activation and ligand recognition.
  • To provide new insights into the structural changes underlying integrin function.

Main Methods:

  • Analysis of three-dimensional structures of integrin extracellular segments.
  • Investigation of integrin cytoplasmic segments and their structural rearrangements.
  • Focus on cation-binding sites and their influence on integrin conformation.

Main Results:

  • Recent advances in structural biology have elucidated integrin tertiary and quaternary structures.
  • New insights into how extracellular cation binding affects integrin conformation.
  • Understanding of structural changes associated with integrin activation and ligand binding.

Conclusions:

  • Structural elucidation of integrins provides a mechanistic basis for their signaling functions.
  • Divalent cations are critical for integrin activation and ligand recognition.
  • Recent structural findings advance our understanding of integrin-dependent cellular processes.