ArticleActa crystallographica. Section D, Structural biology2016
Structures of designed armadillo-repeat proteins show propagation of inter-repeat interface effects.
Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed.
- 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
- Structure of the RSC complex bound to the nucleosome.Science (New York, N.Y.) · 2019Article
- 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
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The armadillo repeat serves as a scaffold for the development of modular peptide-recognition modules. In order to develop such a system, three crystal structures of designed armadillo-repeat proteins with third-generation N-caps (YIII-type), four or five internal repeats (M-type) and second-generation C-caps (AII-type) were determined at 1.8 Å (His-YIIIM4AII), 2.0 Å (His-YIIIM5AII) and 1.95 Å (YIIIM5AII) resolution and compared with those of variants with third-generation C-caps. All constructs are full consensus designs in which the internal repeats have exactly the same sequence, and hence identical conformations of the internal repeats are expected. The N-cap and internal repeats M1 to M3 are indeed extremely similar, but the comparison reveals structural differences in internal repeats M4 and M5 and the C-cap. These differences are caused by long-range effects of the C-cap, contacting molecules in the crystal, and the intrinsic design of the repeat. Unfortunately, the rigid-body movement of the C-terminal part impairs the regular arrangement of internal repeats that forms the putative peptide-binding site. The second-generation C-cap improves the packing of buried residues and thereby the stability of the protein. These considerations are useful for future improvements of an armadillo-repeat-based peptide-recognition system.
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