Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence

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Science  21 Dec 1990:
Vol. 250, Issue 4988, pp. 1712-1715
DOI: 10.1126/science.2148648


lambda Cro is a dimeric DNA binding protein. Random mutagenesis and a selection for Cro activity have been used to identify the contacts between Cro subunits that are crucial for maintenance of a stably folded structure. To obtain equivalent contacts in a monomeric system, a Cro variant was designed and constructed in which the antiparallel beta-ribbon that forms the dimer interface was replaced by a beta-hairpin. The engineered monomer has a folded structure similar to wild type, is significantly more stable than wild type, and exhibits novel half-operator binding activity.

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