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Redesign of the monomer–monomer interface of Cre recombinase yields an obligate heterotetrameric complex

Cre recombinase catalyzes the cleavage and religation of DNA at loxP sites. The enzyme is a homotetramer in its functional state, and the symmetry of the protein complex enforces a pseudo-palindromic symmetry upon the loxP sequence. The Cre-lox system is a powerful tool for many researchers. However...

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Detalles Bibliográficos
Autores principales:	Zhang, Chi, Myers, Connie A., Qi, Zongtai, Mitra, Robi D., Corbo, Joseph C., Havranek, James J.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Oxford University Press 2015
Materias:	Synthetic Biology and Bioengineering
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4605323/ https://www.ncbi.nlm.nih.gov/pubmed/26365240 http://dx.doi.org/10.1093/nar/gkv901

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