ArticleProtein science : a publication of the Protein Society2005
High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Development of mirror-image monobodies targeting the oncogenic BCR::ABL1 kinase.Nature communications · 2024Article
- Engineering an efficient and bright split Corynactis californica green fluorescent protein.Scientific reports · 2021Article
- The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.Biochemistry · 2017Article
- Converting a binding protein into a biosensing conformational switch using protein fragment exchange.Biochemistry · 2014Article
- Thermodynamics, kinetics, and photochemistry of β-strand association and dissociation in a split-GFP system.Journal of the American Chemical Society · 2011Article
- Adnectins: engineered target-binding protein therapeutics.Protein engineering, design & selection : PEDS · 2011Review
- Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.Biochemistry · 2009Article
- High-throughput analysis of the protein sequence-stability landscape using a quantitative yeast surface two-hybrid system and fragment reconstitution.Journal of molecular biology · 2008Article
- Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.Protein science : a publication of the Protein Society · 2007Review
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Authors and funding
4 authors.
Funding
Abstract
The tenth fibronectin type III (FN3) domain of human fibronectin (FNfn10), a prototype of the ubiquitous FN3 domain, is a small, monomeric beta-sandwich protein. In this study, we have bisected FNfn10 in each loop to generate a total of six fragment pairs. We found that fragment pairs bisected at multiple loops of FNfn10 show complementation in vivo as tested with a yeast two-hybrid system. The dissociation constant of these fragment pairs determined in vitro were as low as 3 nM, resulting in one of the tightest fragment complementation systems reported so far. Furthermore, we show that the affinity of fragment complementation is correlated with the stability of the uncut parent protein. Exploring this correlation, we screened a yeast two-hybrid library of one fragment and identified mutations that suppress the effect of a destabilizing mutation in the other fragment. One of the identified mutations significantly increased the stability of the uncut wild-type protein, proving that fragment complementation can be used as a novel strategy for the selection of proteins with enhanced stability.
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