Related Experiment Video

Updated: Aug 8, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

A reassessment of the MAdCAM-1 structure and its role in integrin recognition

J Dando1, K W Wilkinson, S Ortlepp

  • 1Department of Biochemistry, University of Bristol, Bristol BS8 1TD, England.

Acta Crystallographica. Section D, Biological Crystallography
|January 25, 2002
PubMed

Insights

A new crystal structure of mucosal addressin cell-adhesion molecule-1 (MAdCAM-1) reveals altered amino acid conformations critical for ligand binding. This finding suggests MAdCAM-1 oligomerization may influence its role in leukocyte trafficking.

Area of Science:

  • Immunology
  • Structural Biology
  • Cell Biology

Background:

  • Mucosal addressin cell-adhesion molecule-1 (MAdCAM-1) is a key receptor regulating leukocyte trafficking in mucosal tissues.
  • Previous studies confirmed the immunoglobulin superfamily topology of MAdCAM-1's extracellular domains through crystal structure analysis.

Purpose of the Study:

  • To elucidate the structural details of the human MAdCAM-1 amino-terminal domains.
  • To investigate potential structural variations and their impact on MAdCAM-1 function.
  • To explore the possibility of MAdCAM-1 oligomerization.

Main Methods:

  • X-ray crystallography was employed to determine a second crystal structure of the two extracellular amino-terminal domains of human MAdCAM-1.
  • Structural comparison with the previously reported crystal structure was performed.

Main Results:

  • A novel structural conformation was identified in one edge strand of the amino-terminal domain, differing from the previously reported structure.
  • This structural alteration affects the arrangement and conformation of amino acids crucial for ligand binding.
  • The crystal lattice revealed MAdCAM-1 dimers, indicating potential oligomerization.

Conclusions:

  • The identified structural variations in MAdCAM-1 may have implications for its ligand-binding capabilities.
  • The observed dimerization suggests that MAdCAM-1 oligomerization could play a role in its biological functions related to leukocyte adhesion and trafficking.
  • Further research is warranted to fully understand the functional consequences of these structural findings.

More Related Videos

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Dynamic Adhesion Assay for the Functional Analysis of Anti-adhesion Therapies in Inflammatory Bowel Disease08:27

Dynamic Adhesion Assay for the Functional Analysis of Anti-adhesion Therapies in Inflammatory Bowel Disease

Published on: September 20, 2018

Related Concept Videos

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...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
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...
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...