ArticleProtein science : a publication of the Protein Society2014
Crystal structures of designed armadillo repeat proteins: implications of construct design and crystallization conditions on overall structure.
Article in Protein science : a publication of the Protein Society, 2014. 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, 16 citations in OpenAlex.
- HURDLER: a cloning method to overcome length limits in designed repeat proteins.Nucleic acids research · 2026Article
- Unexpected dynamics in femtomolar complexes of binding proteins with peptides.Nature communications · 2023Article
- An automated iterative approach for protein structure refinement using pseudocontact shifts.Journal of biomolecular NMR · 2021Article
- Rigid fusions of designed helical repeat binding proteins efficiently protect a binding surface from crystal contacts.Scientific reports · 2019Article
- Structures of designed armadillo repeat proteins binding to peptides fused to globular domains.Protein science : a publication of the Protein Society · 2017Article
- Beyond Antibodies as Binding Partners: The Role of Antibody Mimetics in Bioanalysis.Annual review of analytical chemistry (Palo Alto, Calif.) · 2017Review
- Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects.Acta crystallographica. Section D, Structural biology · 2016Article
- Article
- Tandem Repeats in Proteins: Prediction Algorithms and Biological Role.Frontiers in bioengineering and biotechnology · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Designed armadillo repeat proteins (dArmRP) are promising modular proteins for the engineering of binding molecules that recognize extended polypeptide chains. We determined the structure of a dArmRP containing five internal repeats and 3rd generation capping repeats in three different states by X-ray crystallography: without N-terminal His6 -tag and in the presence of calcium (YM5 A/Ca(2+) ), without N-terminal His6 -tag and in the absence of calcium (YM5 A), and with N-terminal His6 -tag and in the presence of calcium (His-YM5 A/Ca(2+)). All structures show different quaternary structures and superhelical parameters. His-YM5 A/Ca(2+) forms a crystallographic dimer, which is bridged by the His6 -tag, YM5 A/Ca(2+) forms a domain-swapped tetramer, and only in the absence of calcium and the His6 -tag, YM5 A forms a monomer. The changes of superhelical parameters are a consequence of calcium binding, because calcium ions interact with negatively charged residues, which can also participate in the modulation of helix dipole moments between adjacent repeats. These observations are important for further optimizations of dArmRPs and provide a general illustration of how construct design and crystallization conditions can influence the exact structure of the investigated protein.
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