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...
| Main Authors: | , , , , , |
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| Format: | Online |
| Language: | English |
| Published: |
Oxford University Press
2015
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4605323/ |