ArticleProtein science : a publication of the Protein Society2018
A threonine zipper that mediates protein-protein interactions: Structure and prediction.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Tetrahydrocurcumin targets TRIP13 inhibiting the interaction of TRIP13/USP7/c-FLIP to mediate c-FLIP ubiquitination in triple-negative breast cancer.Journal of advanced research · 2025Article
- Red fluorescent proteins engineered from green fluorescent proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The R882H substitution in the humanThe Journal of biological chemistry · 2019Article
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8 authors.
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Abstract
We present the structure of an engineered protein-protein interface between two beta barrel proteins, which is mediated by interactions between threonine (Thr) residues. This Thr zipper structure suggests that the protein interface is stabilized by close-packing of the Thr residues, with only one intermonomer hydrogen bond (H-bond) between two of the Thr residues. This Thr-rich interface provides a unique opportunity to study the behavior of Thr in the context of many other Thr residues. In previous work, we have shown that the side chain (χ
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