The Constant Domain of CRTAM is Essential for High-affinity Interaction with Nectin-like 2

Overview

Journal Biochem Biophys Rep

Specialty Biochemistry

Date 2024 Sep 12

PMID 39263316

Authors

Juan Carlos Barragan-Galvez

Araceli Hernandez-Flores

Orestes Lopez-Ortega

Adriana A Rodriguez-Alvarez

Jose Luis Maravillas-Montero

Vianney Ortiz-Navarrete

Affiliations

Soon will be listed here.

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.

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