Utrophin ABD binds to F-actin in an open conformation

Structural analyses of actin binding regions comprising tandem calponin homology domains alone and when bound to F-actin have revealed a number of different conformations with calponin homology domains in ‘open’ and ‘closed’ positions. In an attempt to resolve these issues we have examined the prope...

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Detalles Bibliográficos
Autores principales: Broderick, Mike J.F., Bobkov, Andrey, Winder, Steve J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3642092/
https://www.ncbi.nlm.nih.gov/pubmed/23650574
http://dx.doi.org/10.1016/j.fob.2012.01.001

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3642092/
https://www.ncbi.nlm.nih.gov/pubmed/23650574
http://dx.doi.org/10.1016/j.fob.2012.01.001

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