ArticleJournal of the American Chemical Society2010
Evolution of metal selectivity in templated protein interfaces.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 64 citations in OpenAlex.
- Artificial metalloenzymes in complex biological environments.Nature chemical biology · 2026Review
- Zinc-mediated lysosomal activation by 1H10 enhances autophagy and attenuates tau pathology in Alzheimer's disease models.Molecular brain · 2026Article
- The Ascent of Miniproteins.Biochemistry · 2026Review
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- Strand-Swapped SH3 Domain Dimer with Superoxide Dismutase Activity.ACS central science · 2025Article
- Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries.Journal of the American Chemical Society · 2023Article
- Design of a Flexible, Zn-Selective Protein Scaffold that Displays Anti-Irving-Williams Behavior.Journal of the American Chemical Society · 2022Article
- Review
- Redox- and metal-directed structural diversification in designed metalloprotein assemblies.Chemical communications (Cambridge, England) · 2022Article
- Article
- Molecular Approaches to Protein Dimerization: Opportunities for Supramolecular Chemistry.Frontiers in chemistry · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Design of metal-mediated protein assemblies via hydroxamic acid functionalities.Nature protocols · 2021Article
- Symmetry-related residues as promising hotspots for the evolution ofChemical science · 2021Article
- Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites.Angewandte Chemie (International ed. in English) · 2020Article
- A rationally designed peptoid for the selective chelation of ZnChemical science · 2020Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- An efficient, step-economical strategy for the design of functional metalloproteins.Nature chemistry · 2019Article
- Functional protein nanostructures: a chemical toolbox.Chemical Society reviews · 2018Review
- Determining the Structural and Energetic Basis of Allostery in a De Novo Designed Metalloprotein Assembly.Journal of the American Chemical Society · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Selective binding by metalloproteins to their cognate metal ions is essential to cellular survival. How proteins originally acquired the ability to selectively bind metals and evolved a diverse array of metal-centered functions despite the availability of only a few metal-coordinating functionalities remains an open question. Using a rational design approach (Metal-Templated Interface Redesign), we describe the transformation of a monomeric electron transfer protein, cytochrome cb(562), into a tetrameric assembly ((C96)RIDC-1(4)) that stably and selectively binds Zn(2+) and displays a metal-dependent conformational change reminiscent of a signaling protein. A thorough analysis of the metal binding properties of (C96)RIDC-1(4) reveals that it can also stably harbor other divalent metals with affinities that rival (Ni(2+)) or even exceed (Cu(2+)) those of Zn(2+) on a per site basis. Nevertheless, this analysis suggests that our templating strategy simultaneously introduces an increased bias toward binding a higher number of Zn(2+) ions (four high affinity sites) versus Cu(2+) or Ni(2+) (two high affinity sites), ultimately leading to the exclusive selectivity of (C96)RIDC-1(4) for Zn(2+) over those ions. More generally, our results indicate that an initial metal-driven nucleation event followed by the formation of a stable protein architecture around the metal provides a straightforward path for generating structural and functional diversity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.