ArticleThe Journal of biological chemistry2011
A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.
Article in The Journal of biological chemistry, 2011. 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.
- Cryptic genetic variation shapes the fate of gene duplicates in a protein interaction network.Nature communications · 2025Article
- Large-scale survey and database of high affinity ligands for peptide recognition modules.Molecular systems biology · 2020Article
- Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres.Nature microbiology · 2019Article
- Phosphotyrosine signaling proteins that drive oncogenesis tend to be highly interconnected.Molecular & cellular proteomics : MCP · 2013Article
- In situ click chemistry: from small molecule discovery to synthetic antibodies.Integrative biology : quantitative biosciences from nano to macro · 2013Review
- Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathways.The Journal of biological chemistry · 2012Article
- High-throughput analysis of peptide-binding modules.Proteomics · 2012Review
- Distinct peptide binding specificities of Src homology 3 (SH3) protein domains can be determined by modulation of local energetics across the binding interface.The Journal of biological chemistry · 2012Article
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Authors and funding
3 authors.
Funding
Abstract
The yeast Bem1p SH3b and Nbp2p SH3 domains are unusual because they bind to peptides containing the same consensus sequence, yet they perform different functions and display low sequence similarity. In this work, by analyzing the interactions of these domains with six biologically relevant peptides containing the consensus sequence, they are shown to possess finely tuned and distinct binding specificities. We also identify a residue in the Bem1p SH3b domain that inhibits binding, yet is highly conserved for the purpose of preventing nonspecific interactions. Substitution of this residue results in a marked reduction of in vivo function that is caused by titration of the domain away from its proper targets through nonspecific interactions with other proteins. This work provides a clear illustration of the importance of intrinsic binding specificity for the function of protein-protein interaction modules, and the key role of "negative" interactions in determining the specificity of a domain.
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