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

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

Research output: Contribution to journalArticle

28 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)14836-14840
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume109
Issue number37
DOIs
StatePublished - Sep 11 2012

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Keywords

  • Cell adhesion molecule
  • Immunoglobulin superfamily
  • Nectin-2 dimer
  • X-ray crystallography

ASJC Scopus subject areas

  • General

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