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

CRTAM (Class-I MHC restricted T cell-associated molecule) is a member of the Nectin-like family, composed of two extracellular domains, one constant domain (IgC) and another variable domain (IgV), expressed in activated CD8 T cells, epithelial cells, natural killer (NK) cells, and in a subpopulation of CD4 T cells. CRTAM recognizes the ligand Nectin-like 2 (Necl2) through the IgV domain. However, the role of the IgC domain during this ligand recognition has yet to be understood. In this study, we show the purification of soluble-folded Ig domains of CRTAM, and we demonstrate that the IgC domain forms a homodimer in solution via hydrophobic interactions. By surface plasmon resonance (SPR) analysis, we also demonstrate that CRTAM binds to Necl2 with an affinity of 2.16 nM. In conclusion, CRTAM's IgC is essential for a high-affinity interaction with Necl-2.

Authors

Institutions

Publication Details

Journal
Biochemistry and Biophysics Reports
Published
2024-08-25
DOI
https://doi.org/10.1016/j.bbrep.2024.101813
Citations
1
Primary Topic
Immune Cell Function and Interaction
Type
article
Field-Weighted Citation Impact
0.24

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

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

Orestes López‐Ortega, José Luis Maravillas‐Montero, Araceli Hernández‐Flores, Juan Carlos Barragán‐Gálvez et al.
1 citations
Biochemistry and Biophysics Reports
Immune Cell Function and Interaction
0.24
article

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

Orestes López‐Ortega, José Luis Maravillas‐Montero, Araceli Hernández‐Flores, Juan Carlos Barragán‐Gálvez, Vianney Ortiz‐Navarrete, Adriana A. Rodriguez-Alvarez
article en
1 citations

Abstract

CRTAM (Class-I MHC restricted T cell-associated molecule) is a member of the Nectin-like family, composed of two extracellular domains, one constant domain (IgC) and another variable domain (IgV), expressed in activated CD8 T cells, epithelial cells, natural killer (NK) cells, and in a subpopulation of CD4 T cells. CRTAM recognizes the ligand Nectin-like 2 (Necl2) through the IgV domain. However, the role of the IgC domain during this ligand recognition has yet to be understood. In this study, we show the purification of soluble-folded Ig domains of CRTAM, and we demonstrate that the IgC domain forms a homodimer in solution via hydrophobic interactions. By surface plasmon resonance (SPR) analysis, we also demonstrate that CRTAM binds to Necl2 with an affinity of 2.16 nM. In conclusion, CRTAM's IgC is essential for a high-affinity interaction with Necl-2.

Biochemistry and Biophysics ReportsVol. 39
Boston University (US), Centre National de la Recherche Scientifique (FR), Universidad de Guanajuato (MX), Inserm (FR), Université Paris Cité (FR), Institut Necker Enfants Malades (FR), Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán (MX), Universidad de la Sierra (MX), Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (MX), Universidad Nacional Autónoma de México (MX)
Consejo Nacional de Ciencia y Tecnología, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional
Zero hunger
Openalex Percentile: Top 43%
Immune Cell Function and Interaction
0.24
DOIOpen Access PDFOpenAlex
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.