Structural highlights
Publication Abstract from PubMed
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 A 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.
Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion.,Samanta D, Ramagopal UA, Rubinstein R, Vigdorovich V, Nathenson SG, Almo SC Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14836-40. Epub 2012 Aug 27. PMID:22927415[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Samanta D, Ramagopal UA, Rubinstein R, Vigdorovich V, Nathenson SG, Almo SC. Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion. Proc Natl Acad Sci U S A. 2012 Sep 11;109(37):14836-40. Epub 2012 Aug 27. PMID:22927415 doi:http://dx.doi.org/10.1073/pnas.1212912109