ArticlePloS one2012
Differential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- How a highly acidic SH3 domain folds in the absence of its charged peptide target.Protein science : a publication of the Protein Society · 2023Article
- Structural features of Dnase1L3 responsible for serum antigen clearance.Communications biology · 2022Article
- A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.PLoS computational biology · 2020Article
- Cyclophilin A allows the allosteric regulation of a structural motif in the disordered domain 2 of NS5A and thereby fine-tunes HCV RNA replication.The Journal of biological chemistry · 2019Article
- Site-specific 2D IR spectroscopy: a general approach for the characterization of protein dynamics with high spatial and temporal resolution.Physical chemistry chemical physics : PCCP · 2019Article
- A multi-column plate adapter provides an economical and versatile high-throughput protein purification system.Protein expression and purification · 2018Article
- Molecular Mechanisms of Tight Binding through Fuzzy Interactions.Biophysical journal · 2018Article
- Article
- The PROSECCO server for chemical shift predictions in ordered and disordered proteins.Journal of biomolecular NMR · 2017Article
- Resolution of Site-Specific Conformational Heterogeneity in Proline-Rich Molecular Recognition by Src Homology 3 Domains.Journal of the American Chemical Society · 2016Article
- Article
- Secondary Structure Analysis of a Functional Construct of Caveolin-1 Reveals a Long C-Terminal Helix.Biophysical journal · 2015Article
- Differential Recognition Preferences of the Three Src Homology 3 (SH3) Domains from the Adaptor CD2-associated Protein (CD2AP) and Direct Association with Ras and Rab Interactor 3 (RIN3).The Journal of biological chemistry · 2015Article
- Characterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25.Nucleic acids research · 2015Article
- A tool set to map allosteric networks through the NMR chemical shift covariance analysis.Scientific reports · 2014Article
- NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.Physical chemistry chemical physics : PCCP · 2014Article
- A semi-automated method for purification of milligram quantities of proteins on the QIAcube.Protein expression and purification · 2014Article
- The cytoplasmic domain of the T-cell receptor zeta subunit does not form disordered dimers.Journal of molecular biology · 2014Article
- Allosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTR.PloS one · 2013Article
- Site-selective Characterization of Src Homology 3 Domain Molecular Recognition with Cyanophenylalanine Infrared Probes.Analytical methods : advancing methods and applicationsArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
There is increasing evidence for the functional importance of multiple dynamically populated states within single proteins. However, peptide binding by protein-protein interaction domains, such as the SH3 domain, has generally been considered to involve the full engagement of peptide to the binding surface with minimal dynamics and simple methods to determine dynamics at the binding surface for multiple related complexes have not been described. We have used NMR spectroscopy combined with isothermal titration calorimetry to comprehensively examine the extent of engagement to the yeast Abp1p SH3 domain for 24 different peptides. Over one quarter of the domain residues display co-linear chemical shift perturbation (CCSP) behavior, in which the position of a given chemical shift in a complex is co-linear with the same chemical shift in the other complexes, providing evidence that each complex exists as a unique dynamic rapidly inter-converting ensemble. The extent the specificity determining sub-surface of AbpSH3 is engaged as judged by CCSP analysis correlates with structural and thermodynamic measurements as well as with functional data, revealing the basis for significant structural and functional diversity amongst the related complexes. Thus, CCSP analysis can distinguish peptide complexes that may appear identical in terms of general structure and percent peptide occupancy but have significant local binding differences across the interface, affecting their ability to transmit conformational change across the domain and resulting in functional differences.
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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.