Cargando…
High Affinity vs. Native Fibronectin in the Modulation of αvβ3 Integrin Conformational Dynamics: Insights from Computational Analyses and Implications for Molecular Design
Understanding how binding events modulate functional motions of multidomain proteins is a major issue in chemical biology. We address several aspects of this problem by analyzing the differential dynamics of αvβ3 integrin bound to wild type (wtFN10, agonist) or high affinity (hFN10, antagonist) muta...
Autores principales: | Paladino, Antonella, Civera, Monica, Belvisi, Laura, Colombo, Giorgio |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5293283/ https://www.ncbi.nlm.nih.gov/pubmed/28114375 http://dx.doi.org/10.1371/journal.pcbi.1005334 |
Ejemplares similares
-
Structural insights into integrin α(5)β(1) opening by fibronectin ligand
por: Schumacher, Stephanie, et al.
Publicado: (2021) -
Insights into the Binding of Cyclic RGD Peptidomimetics to α(5)β(1) Integrin by using Live‐Cell NMR And Computational Studies
por: Guzzetti, Ileana, et al.
Publicado: (2016) -
Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change
por: Su, Yang, et al.
Publicado: (2022) -
Structural basis for pure antagonism of integrin αVβ3 by a high affinity form of fibronectin
por: Van Agthoven, Johannes F., et al.
Publicado: (2014) -
Conformational equilibria and intrinsic affinities define integrin activation
por: Li, Jing, et al.
Publicado: (2017)