Dynamic profile analysis to characterize dynamics-driven allosteric sites in enzymes

We examine the dynamic features of non-trivial allosteric binding sites to elucidate potential drug binding sites. These allosteric sites were previously found to be allosteric after determination of the protein-drug co-crystal structure. After comprehensive search in the Protein Data Bank, we ident...

Descripción completa

Detalles Bibliográficos
Autores principales: Taguchi, Junko, Kitao, Akio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2016
Materias:
Regular Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5042162/
https://www.ncbi.nlm.nih.gov/pubmed/27924265
http://dx.doi.org/10.2142/biophysico.13.0_117

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5042162/
https://www.ncbi.nlm.nih.gov/pubmed/27924265
http://dx.doi.org/10.2142/biophysico.13.0_117

Ejemplares similares