ArticleProceedings of the National Academy of Sciences of the United States of America2003
Lanthanide-binding helix-turn-helix peptides: solution structure of a designed metallonuclease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 60 citations in OpenAlex.
- Machine Learning-Based Development of Gadolinium Binding Peptides.NMR in biomedicine · 2026Article
- Machine learning-based development of Gadolinium binding peptides.bioRxiv : the preprint server for biology · 2025Article
- Lanmodulin peptides - unravelling the binding of the EF-Hand loop sequences stripped from the structural corset.Inorganic chemistry frontiers · 2022Article
- Quantitative Assessment of Chirality of Protein Secondary Structures and Phenylalanine Peptide Nanotubes.Nanomaterials (Basel, Switzerland) · 2021Article
- Computational Simulation of Holin S105 in Membrane Bilayer and Its Dimerization Through a Helix-Turn-Helix Motif.The Journal of membrane biology · 2021Article
- Lanthanide-Based Optical Probes of Biological Systems.Cell chemical biology · 2020Review
- DNA targeting and cleavage by an engineered metalloprotein dimer.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Incorporating electron-transfer functionality into synthetic metalloproteins from the bottom-up.Inorganic chemistry · 2006Article
- Engineered lanthanide-binding metallohomeodomains: designing folded chimeras by modular turn substitution.Protein science : a publication of the Protein Society · 2006Article
- Sequence preference in DNA binding: de novo designed helix-turn-helix metallopeptides recognize a family of DNA target sites.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2006Article
- Biological inorganic chemistry at the beginning of the 21st century.Proceedings of the National Academy of Sciences of the United States of America · 2003Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A designed lanthanide-binding chimeric peptide based on the strikingly similar geometries of the EF-hand and helix-turn-helix (HTH) motifs was investigated by NMR and CD spectroscopy and found to retain the same overall solution structure of the parental motifs. CD spectroscopy showed that the 33-mer peptide P3W folds on binding lanthanides, with an increase in alpha-helicity from 20% in the absence of metal to 38% and 35% in the presence of excess Eu(III) and La(III) ions, respectively. The conditional binding affinities of P3W for La(III) (5.9 +/- 0.3 microM) and for Eu(III) (6.2 +/- 0.3 microM) (pH 7.8, 5 mM Tris) were determined by tryptophan fluorescence titration. The La(III) complex of peptide P3, which differs from P3W by only one Trp-to-His substitution, has much less signal dispersion in the proton NMR spectra than LaP3W, indicating that the Trp residue is a critical hydrophobic anchor for maintaining a well-folded helix-turn-helix structure. A chemical-shift index analysis indicates the metallopeptide has a helix-loop-helix secondary structure. A structure calculated by using nuclear Overhauser effect and other NMR constraints reveals that P3W not only has a tightly folded metal-binding loop but also retains the alpha-alpha corner supersecondary structure of the parental motifs. Although the solution structure is undefined at both the N and C termini, the NMR structure confirms the successful incorporation of a metal-binding loop into a HTH sequence.
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