ArticleNucleic acids research2009
Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Fragment-Based Approaches to Identify RNA Binders.Journal of medicinal chemistry · 2023Review
- All Domains of SARS-CoV-2 nsp1 Determine Translational Shutoff and Cytotoxicity of the Protein.Journal of virology · 2023Article
- Fragment-Based Drug Discovery by NMR. Where Are the Successes and Where can It Be Improved?Frontiers in molecular biosciences · 2022Article
- Structural and Functional Characterization of Host FHL1 Protein Interaction with Hypervariable Domain of Chikungunya Virus nsP3 Protein.Journal of virology · 2020Article
- Article
- Interaction Between the a3 Region of Factor VIII and the TIL'E' Domains of the von Willebrand Factor.Biophysical journal · 2019Article
- Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- 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
- Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.The FEBS journal · 2014Review
- Allosteric communication in the KIX domain proceeds through dynamic repacking of the hydrophobic core.ACS chemical biology · 2013Article
- Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.PloS one · 2013Article
- Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics.Angewandte Chemie (International ed. in English) · 2012Article
- Characterizing weak protein-protein complexes by NMR residual dipolar couplings.European biophysics journal : EBJ · 2011Review
- Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins.Journal of biomolecular NMR · 2011Article
- Fast approximations of the rotational diffusion tensor and their application to structural assembly of molecular complexes.Proteins · 2011Article
- Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.Journal of biomolecular NMR · 2011Article
- Structural NMR of protein oligomers using hybrid methods.Journal of structural biology · 2011Review
- Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping.Protein science : a publication of the Protein Society · 2010Article
- Structural assembly of molecular complexes based on residual dipolar couplings.Journal of the American Chemical Society · 2010Article
- Solution structure of the IIAChitobiose-IIBChitobiose complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system.The Journal of biological chemistry · 2010Article
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6 authors.
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Abstract
The description of the interactome represents one of key challenges remaining for structural biology. Physiologically important weak interactions, with dissociation constants above 100 muM, are remarkably common, but remain beyond the reach of most of structural biology. NMR spectroscopy, and in particular, residual dipolar couplings (RDCs) provide crucial conformational constraints on intermolecular orientation in molecular complexes, but the combination of free and bound contributions to the measured RDC seriously complicates their exploitation for weakly interacting partners. We develop a robust approach for the determination of weak complexes based on: (i) differential isotopic labeling of the partner proteins facilitating RDC measurement in both partners; (ii) measurement of RDC changes upon titration into different equilibrium mixtures of partially aligned free and complex forms of the proteins; (iii) novel analytical approaches to determine the effective alignment in all equilibrium mixtures; and (iv) extraction of precise RDCs for bound forms of both partner proteins. The approach is demonstrated for the determination of the three-dimensional structure of the weakly interacting CD2AP SH3-C:Ubiquitin complex (K(d) = 132 +/- 13 muM) and is shown, using cross-validation, to be highly precise. We expect this methodology to extend the remarkable and unique ability of NMR to study weak protein-protein complexes.
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