ArticleCurrent research in structural biology2021
Integrated analysis of Shank1 PDZ interactions with C-terminal and internal binding motifs.
Article in Current research in structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- An Atlas of Short Linear Motif-Mediated Human Protein-Protein Interactions.bioRxiv : the preprint server for biology · 2026Article
- Discovery of SHANK1-PDZ Peptide-Fragment Inhibitors Using a Dynamic Ligation Screening Strategy.Biochemistry · 2026Article
- Article
- Biophysical and structural analyses of the interaction between the SHANK1 PDZ domain and an internal SLiM.The Biochemical journal · 2024Article
- Simulated complexes formed from a set of postsynaptic proteins suggest a localised effect of a hypomorphic Shank mutation.BMC neuroscience · 2024Article
- Unconventional PDZ Recognition Revealed in α7 nAChR-PICK1 Complexes.ACS chemical neuroscience · 2024Article
- Dishevelled2 activates WGEF via its interaction with a unique internal peptide motif of the GEF.Communications biology · 2024Article
- Resonance assignment of the Shank1 PDZ domain.Biomolecular NMR assignments · 2022Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
PDZ domains constitute a large family of modular domains that are well-known for binding C-terminal motifs of target proteins. Some of them also bind to internal PDZ binding motifs (PDZbms), but this aspect of the PDZ interactome is poorly studied. Here we explored internal PDZbm-mediated interactions using the PDZ domain of Shank1 as a model. We identified a series of human Shank1 ligands with C-terminal or internal PDZbms using proteomic peptide-phage display, and established that while the consensus sequence of C-terminal ligands is x-T-x-(L/F)-COOH, the consensus of internal PDZbm is exclusively x-T-x-F-x, where x is any amino acid. We found that the affinities of PDZbm interactions are in the low micromolar range. The crystal structure of the complex between Shank1 PDZ and an internal PDZbm revealed that the binding mode of internal PDZbms was similar to that of C-terminal ligands. Pull-down experiments confirmed that both C-terminal and internal PDZbm interactions can occur in the context of full-length proteins. Our study expands the interactome of Shank1 and hints at a largely unexplored interaction space of PDZ domains.
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