“DFG-Flip” in the Insulin Receptor Kinase Is Facilitated by a Helical Intermediate State of the Activation Loop

We have characterized a large-scale inactive-to-active conformational change in the activation-loop of the insulin receptor kinase domain at the atomistic level via untargeted temperature-accelerated molecular dynamics (TAMD) and free-energy calculations using the string method. TAMD simulations con...

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Detalles Bibliográficos
Main Authors: Vashisth, Harish, Maragliano, Luca, Abrams, Cameron F.
Formato: Artigo
Idioma:Inglês
Publicado: The Biophysical Society 2012
Assuntos:
Protein
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC3328698/
https://ncbi.nlm.nih.gov/pubmed/22768955
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2012.03.031
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