Structural and energetic determinants of adhesive binding specificity in type I cadherins

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 111; no. 40; p. 14322
• Main Authors: Vendome, Jeremie, Felsovalyi, Klara, Song, Hang, Yang, Zhongyu, Jin, Xiangshu, Brasch, Julia, Harrison, Oliver J., Ahlsen, Goran, Bahna, Fabiana, Kaczynska, Anna, Katsamba, Phinikoula S., Edmond, Darwin, Hubbell, Wayne L., Shapiro, Lawrence, Honig, Barry
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 07.10.2014; National Acad Sciences
• Series: PNAS Plus
• Subjects: Amino Acid Sequence; Animals; binding capacity; Binding sites; Binding, Competitive; Biological Sciences; cadherins; Cadherins - chemistry; Cadherins - genetics; Cadherins - metabolism; cell adhesion; Cell adhesion & migration; Crystallography; Crystallography, X-Ray; dimerization; Electron Spin Resonance Spectroscopy; Electrons; Evolution; HEK293 Cells; Heterogeneity; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Mice; Models, Molecular; Molecular Sequence Data; Molecular structure; Mutation; PNAS Plus; PNAS PLUS Significance Statements; Protein Binding; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins; Resonance; Sequence Homology, Amino Acid; Static Electricity; Xenopus; Xenopus Proteins - chemistry; Xenopus Proteins - genetics; Xenopus Proteins - metabolism; entropy contribution; protein family design; cadherin dimerization

Type I cadherins comprise a family of cell–cell adhesion proteins that dimerize in a highly specific fashion. There are small differences in dimerization affinities among family members that are evolutionarily conserved and that have profound effects on cell-patterning behavior. There are few exampl...