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The constant domain of CRTAM is essential for high-affinity interaction with Nectin-like 2.
Barragan-Galvez, Juan Carlos; Hernandez-Flores, Araceli; Lopez-Ortega, Orestes; Rodriguez-Alvarez, Adriana A; Maravillas-Montero, Jose Luis; Ortiz-Navarrete, Vianney.
Affiliation
  • Barragan-Galvez JC; Department of Molecular Biomedicine, Center for Research and Advanced Studies (CINVESTAV), Mexico City, Mexico.
  • Hernandez-Flores A; Departamento de Farmacia, División de Ciencias Naturales y Exactas, Universidad de Guanajuato, Guanajuato, 36200, Mexico.
  • Lopez-Ortega O; Universidad de la Sierra Sur, Miahuatlán de Porfirio Díaz, Oaxaca, Mexico.
  • Rodriguez-Alvarez AA; Université Paris Cité, INSERM UMR-S1151, CNRS UMR-S8253, Institut Necker Enfants Malades, 75015, Paris, France.
  • Maravillas-Montero JL; Boston University School of Medicine, 72 E Concord St, Boston, MA, 02118, United States.
  • Ortiz-Navarrete V; Research Support Network, Universidad Nacional Autónoma de México and Instituto Nacional de Ciencias Médicas y Nutrición "Salvador Zubirán", Mexico City, Mexico.
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.
Key words

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

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