ArticleInorganic chemistry2010
Modular and versatile hybrid coordination motifs on alpha-helical protein surfaces.
Article in Inorganic chemistry, 2010. 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, 20 citations in OpenAlex.
- Design of metal-mediated protein assemblies via hydroxamic acid functionalities.Nature protocols · 2021Article
- Article
- Stable and Potent Selenomab-Drug Conjugates.Cell chemical biology · 2017Article
- Tunable Helicity, Stability and DNA-Binding Properties of Short Peptides with Hybrid Metal Coordination Motifs.Chemical science · 2016Article
- Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker.Nature communications · 2016Article
- Metal-Directed Design of Supramolecular Protein Assemblies.Methods in enzymology · 2016Article
- Functional, metal-based crosslinkers for α-helix induction in short peptides.Chemical science · 2013Article
- Conformational Study of an Artificial Metal-Dependent Regulation Site for Use in Designer Proteins.Zeitschrift fur anorganische und allgemeine Chemie · 2013Article
- An approach to crystallizing proteins by metal-mediated synthetic symmetrization.Protein science : a publication of the Protein Society · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We report here the construction of phenanthroline (Phen) and terpyridine (Terpy)-based hybrid coordination motifs (HCMs), which were installed on the surface of the four-helical bundle hemeprotein cytochrome cb(562). The resulting constructs, termed HPhen1, HPhen2, HPhen3, and HTerpy1, feature HCMs that are composed of a histidine ligand and a Phen or Terpy functionality located two helix turns away, yielding stable tri- or tetradentate coordination platforms. Our characterization of the tridentate HCMs indicates that they accommodate many divalent metal ions (Co(2+), Ni(2+), Cu(2+), Zn(2+)) with nanomolar to femtomolar affinities, lead to significant stabilization of the alpha-helical protein scaffold through metal-mediated cross-linking, assert tight control over protein dimerization, and provide stable and high-affinity binding sites for substitution-inert metal probes. Our analyses suggest that such tridentate HCMs may be used modularly on any alpha-helical protein surface in a sequence-independent fashion.
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