Related Experiment Video

Updated: Jun 13, 2025

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

5.9K

The constant domain of CRTAM is essential for high-affinity interaction with Nectin-like 2

Juan Carlos Barragan-Galvez1,2, Araceli Hernandez-Flores3, Orestes Lopez-Ortega4

  • 1Department of Molecular Biomedicine, Center for Research and Advanced Studies (CINVESTAV), Mexico City, Mexico.

Biochemistry and Biophysics Reports
|September 12, 2024
PubMed

Insights

Class-I MHC restricted T cell-associated molecule (CRTAM) interaction with Necl2 is crucial. The study reveals CRTAM's IgC domain is essential for high-affinity binding to Necl2, impacting T cell recognition.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Class-I MHC restricted T cell-associated molecule (CRTAM) is a Nectin-like family member expressed on immune cells.
  • CRTAM has two extracellular domains: IgC and IgV, with IgV mediating ligand recognition.
  • The function of the IgC domain in CRTAM-ligand interaction remains unclear.

Purpose of the Study:

  • To investigate the role of the IgC domain in CRTAM-ligand binding.
  • To characterize the biophysical properties of CRTAM's Ig domains.

Main Methods:

  • Purification of soluble, folded Ig domains of CRTAM.
  • Surface Plasmon Resonance (SPR) analysis to determine binding affinity.

Main Results:

  • The IgC domain of CRTAM forms a homodimer in solution through hydrophobic interactions.
  • CRTAM exhibits a high-affinity interaction with Nectin-like 2 (Necl2), with an affinity of 2.16 nM.

Conclusions:

  • The IgC domain of CRTAM is essential for high-affinity binding to Necl2.
  • This finding provides insight into the molecular mechanisms of CRTAM-mediated cell interactions.

Keywords:
AffinityCADM1CRTAMConstant domainDimerNectin-like 2

More Related Videos

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.3K
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

10.5K

Related Concept Videos

Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
4.7K
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...
3.3K
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...
3.2K
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
2.3K
Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
5.2K
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
3.7K