Cargando…
Molecular design principles underlying β-strand swapping in the adhesive dimerization of cadherins
Cell adhesion by classical cadherins is mediated by dimerization of their EC1 domains through the “swapping” of N-terminal β-strands. We use molecular simulations, measurements of binding affinities, and x-ray crystallography to provide a detailed picture of the structural and energetic factors that...
Autores principales: | Vendome, Jeremie, Posy, Shoshana, Jin, Xiangshu, Bahna, Fabiana, Ahlsen, Goran, Shapiro, Lawrence, Honig, Barry |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3113550/ https://www.ncbi.nlm.nih.gov/pubmed/21572446 http://dx.doi.org/10.1038/nsmb.2051 |
Ejemplares similares
-
Nectin ectodomain structures reveal a canonical adhesive interface
por: Harrison, Oliver J., et al.
Publicado: (2012) -
Transforming binding affinities from 3D to 2D with application to cadherin clustering
por: Wu, Yinghao, et al.
Publicado: (2011) -
Multiple dimeric structures and strand-swap dimerization of E-cadherin in solution visualized by high-speed atomic force microscopy
por: Nishiguchi, Shigetaka, et al.
Publicado: (2022) -
Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior
por: Brasch, Julia, et al.
Publicado: (2018) -
Molecular basis of sidekick-mediated cell-cell adhesion and specificity
por: Goodman, Kerry M, et al.
Publicado: (2016)