ArticleProtein & cell2011
Engineering a zinc binding site into the de novo designed protein DS119 with a βαβ structure.
Article in Protein & cell, 2011. 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.
- Fluctuating β-Sheet Secondary Structure in DS119 Explains the Small Effects of Backbone N-Amination on Thermal Stability.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
- An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023Article
- Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.Journal of the American Chemical Society · 2019Article
- Computational approaches forBioscience reports · 2017Review
- Rational design of TNFα binding proteins based on the de novo designed protein DS119.Protein science : a publication of the Protein Society · 2016Article
- Designing hydrolytic zinc metalloenzymes.Biochemistry · 2014Review
- Slow and bimolecular folding of a de novo designed monomeric protein DS119.Biophysical journal · 2013Article
- Designing functional metalloproteins: from structural to catalytic metal sites.Coordination chemistry reviews · 2013Article
- Influence of active site location on catalytic activity in de novo-designed zinc metalloenzymes.Journal of the American Chemical Society · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional proteins designed de novo have potential application in chemical engineering, agriculture and healthcare. Metal binding sites are commonly used to incorporate functions. Based on a de novo designed protein DS119 with a βαβ structure, we have computationally engineered zinc binding sites into it using a home-made searching program. Seven out of the eight designed sequences tested were shown to bind Zn(2+) with micromolar affinity, and one of them bound Zn(2+) with 1:1 stoichiometry. This is the first time that metalloproteins with an α, β mixed structure have been designed from scratch.
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Registered trials
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