Work

Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell–cell adhesion

Year: 2012

Type: article

Abstract: Nectins are members of the Ig superfamily that mediate cell-cell adhesion through homophilic and heterophilic interactions. We have determined the crystal structure of the nectin-2 homodimer at 1.3 Å resolution. Structural analysis and complementary mutagenesis studies reveal the basis for recognition and selectivity among the nectin family members. Notably, the close proximity of charged residues at the dimer interface is a major determinant of the binding affinities associated with homophilic and heterophilic interactions within the nectin family. Our structural and biochemical data provide a mechanistic basis to explain stronger heterophilic versus weaker homophilic interactions among these family members and also offer insights into nectin-mediated transinteractions between engaging cells.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1212912109

Authors: Dibyendu Samanta, Udupi A. Ramagopal, Rotem Rubinstein, Vladimir Vigdorovich, Stanley G. Nathenson, Steven C. Almo

Institution: Albert Einstein College of Medicine

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

Open Access status: green

Funders: National Cancer Institute, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases