The constant domain of CRTAM is essential for high-affinity interaction with Nectin-like 2.
Biochem Biophys Rep
; 39: 101813, 2024 Sep.
Article
in En
| MEDLINE
| ID: mdl-39263316
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Biochem Biophys Rep
Year:
2024
Document type:
Article
Affiliation country:
Mexico
Country of publication:
Netherlands