Cargando…
Dynamics Govern Specificity of a Protein-Protein Interface: Substrate Recognition by Thrombin
Biomolecular recognition is crucial in cellular signal transduction. Signaling is mediated through molecular interactions at protein-protein interfaces. Still, specificity and promiscuity of protein-protein interfaces cannot be explained using simplistic static binding models. Our study rationalizes...
Autores principales: | Fuchs, Julian E., Huber, Roland G., Waldner, Birgit J., Kahler, Ursula, von Grafenstein, Susanne, Kramer, Christian, Liedl, Klaus R. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4619833/ https://www.ncbi.nlm.nih.gov/pubmed/26496636 http://dx.doi.org/10.1371/journal.pone.0140713 |
Ejemplares similares
-
Specificity of a protein–protein interface: Local dynamics direct substrate recognition of effector caspases
por: Fuchs, Julian E., et al.
Publicado: (2014) -
Specificity of a protein–protein interface: Local dynamics direct substrate recognition of effector caspases
por: Fuchs, Julian E, et al.
Publicado: (2014) -
Quantitative Correlation of Conformational Binding
Enthalpy with Substrate Specificity of Serine Proteases
por: Waldner, Birgit J., et al.
Publicado: (2015) -
Electrostatic recognition in substrate binding to serine proteases
por: Waldner, Birgit J., et al.
Publicado: (2018) -
Substrate-Driven Mapping of the Degradome by Comparison of Sequence Logos
por: Fuchs, Julian E., et al.
Publicado: (2013)