Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell–cell adhesion
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- Dibyendu Samanta
- Departments of aMicrobiology and Immunology,
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- Udupi A. Ramagopal
- Biochemistry,
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- Rotem Rubinstein
- Biochemistry,
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- Vladimir Vigdorovich
- Departments of aMicrobiology and Immunology,
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- Stanley G. Nathenson
- Departments of aMicrobiology and Immunology,
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- Steven C. Almo
- Biochemistry,
書誌事項
- 公開日
- 2012-08-27
- DOI
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- 10.1073/pnas.1212912109
- 公開者
- Proceedings of the National Academy of Sciences
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説明
<jats:p>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.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 109 (37), 14836-14840, 2012-08-27
Proceedings of the National Academy of Sciences
