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Protein X-ray crystallography of the 14-3-3ζ/SOS1 complex

Activation of Ras-MAPK signaling regulates essential cellular functions; its aberration leads to irregular cell proliferation and differentiation (i.e. pancreatic cancer). Previously, it was revealed that the formation of the complex of the 14-3-3 protein and the Son of sevenless homolog 1 (SOS1) -...

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Detalles Bibliográficos
Autores principales: Ballone, Alice, Centorrino, Federica, Wolter, Madita, Ottmann, Christian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6141376/
https://www.ncbi.nlm.nih.gov/pubmed/30229043
http://dx.doi.org/10.1016/j.dib.2018.06.060
Descripción
Sumario:Activation of Ras-MAPK signaling regulates essential cellular functions; its aberration leads to irregular cell proliferation and differentiation (i.e. pancreatic cancer). Previously, it was revealed that the formation of the complex of the 14-3-3 protein and the Son of sevenless homolog 1 (SOS1) - one of the main actors of the Ras-MAPK cascade -, would represent a key-process to downstream the deviant Ra-MAPK signaling. In this data article we attempt to shed some light on the 3D structure, providing useful details about the crystallization process of the 14-3-3ζ dimer in complex with the 13-mer SOS1pS(1161). The crystal structure is deposited at the Protein Data Bank with identifier 6F08. This Data in Brief article refers to “Structural characterization of 14-3-3ζ in complex with the human Son of sevenless homolog 1 (SOS1) (2018).”