ArticleJournal of molecular biology2007
Structural basis for ubiquitin recognition by SH3 domains.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Mechanism of beta-arrestin 1 mediated Src activation via Src SH3 domain revealed by cryo-electron microscopy.Nature communications · 2026Article
- Mechanism of beta-arrestin 1 mediated Src activation via Src SH3 domain revealed by cryo-electron microscopy.bioRxiv : the preprint server for biology · 2025Article
- Synthesis of SelectivelyChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- The conformation of the nSrc specificity-determining loop in the Src SH3 domain is modulated by a WX conserved sequence motif found in SH3 domains.Frontiers in molecular biosciences · 2024Article
- SH3 domain regulation of RhoGAP activity: Crosstalk between p120RasGAP and DLC1 RhoGAP.Nature communications · 2022Article
- A litmus test for classifying recognition mechanisms of transiently binding proteins.Nature communications · 2022Article
- Article
- Regulation of CYLD activity and specificity by phosphorylation and ubiquitin-binding CAP-Gly domains.Cell reports · 2021Article
- Article
- Mechanism of recruitment and activation of the endosome-associated deubiquitinase AMSH.Biochemistry · 2013Article
- An introduction to biological NMR spectroscopy.Molecular & cellular proteomics : MCP · 2013Review
- Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.PloS one · 2013Article
- Ubiquitin and its binding domains.Frontiers in bioscience (Landmark edition) · 2012Review
- Characterization of domain-peptide interaction interface: prediction of SH3 domain-mediated protein-protein interaction network in yeast by generic structure-based models.Journal of proteome research · 2012Article
- Characterizing weak protein-protein complexes by NMR residual dipolar couplings.European biophysics journal : EBJ · 2011Review
- Host sequence motifs shared by HIV predict response to antiretroviral therapy.BMC medical genomics · 2009Article
- Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex.Nucleic acids research · 2009Article
- Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain.Journal of molecular biology · 2009Article
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Authors and funding
3 authors.
Funding
Abstract
The SH3 domain is a protein-protein interaction module commonly found in intracellular signaling and adaptor proteins. The SH3 domains of multiple endocytic proteins have been recently implicated in binding ubiquitin, which serves as a signal for diverse cellular processes including gene regulation, endosomal sorting, and protein destruction. Here we describe the solution NMR structure of ubiquitin in complex with an SH3 domain belonging to the yeast endocytic protein Sla1. The ubiquitin binding surface of the Sla1 SH3 domain overlaps substantially with the canonical binding surface for proline-rich ligands. Like many other ubiquitin-binding motifs, the SH3 domain engages the Ile44 hydrophobic patch of ubiquitin. A phenylalanine residue located at the heart of the ubiquitin-binding surface of the SH3 domain serves as a key specificity determinant. The structure of the SH3-ubiquitin complex explains how a subset of SH3 domains has acquired this non-traditional function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.