ArticleJournal of biomolecular NMR2010
PCS-based structure determination of protein-protein complexes.
Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- HECT domain interaction with ubiquitin binding sites on Tsg101-UEV controls HIV-1 egress, maturation, and infectivity.The Journal of biological chemistry · 2023Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- YAPPIS-Finder: A novel method for protein-protein interaction site predictions.Bioinformation · 2022Article
- Phosphoserine for the generation of lanthanide-binding sites on proteins for paramagnetic nuclear magnetic resonance spectroscopy.Magnetic resonance (Gottingen, Germany) · 2021Article
- Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020Review
- Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake.Nature communications · 2020Article
- Integrative Protein Modeling in RosettaNMR from Sparse Paramagnetic Restraints.Structure (London, England : 1993) · 2019Article
- Oligomer Model of PB1 Domain of p62/SQSTM1 Based on Crystal Structure of Homo-Dimer and Calculation of Helical Characteristics.Molecules and cells · 2019Article
- Surveying the landscape of optogenetic methods for detection of protein-protein interactions.Wiley interdisciplinary reviews. Systems biology and medicine · 2018Review
- Long-range paramagnetic NMR data can provide a closer look on metal coordination in metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Verteporfin-induced formation of protein cross-linked oligomers and high molecular weight complexes is mediated by light and leads to cell toxicity.Scientific reports · 2017Article
- Genetic visualization of protein interactions harnessing liquid phase transitions.Scientific reports · 2017Article
- Modern Technologies of Solution Nuclear Magnetic Resonance Spectroscopy for Three-dimensional Structure Determination of Proteins Open Avenues for Life Scientists.Computational and structural biotechnology journal · 2017Review
- A new carbamidemethyl-linked lanthanoid chelating tag for PCS NMR spectroscopy of proteins in living HeLa cells.Journal of biomolecular NMR · 2016Article
- "Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.ChemistryOpen · 2016Review
- Structure biology of selective autophagy receptors.BMB reports · 2016Review
- Ligand-driven conformational changes of MurD visualized by paramagnetic NMR.Scientific reports · 2015Article
- Paramagnetic Ligand Tagging To Identify Protein Binding Sites.Journal of the American Chemical Society · 2015Article
- Compact, hydrophilic, lanthanide-binding tags for paramagnetic NMR spectroscopy.Chemical science · 2015Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A simple and fast nuclear magnetic resonance method for docking proteins using pseudo-contact shift (PCS) and (1)H(N)/(15)N chemical shift perturbation is presented. PCS is induced by a paramagnetic lanthanide ion that is attached to a target protein using a lanthanide binding peptide tag anchored at two points. PCS provides long-range (approximately 40 A) distance and angular restraints between the lanthanide ion and the observed nuclei, while the (1)H(N)/(15)N chemical shift perturbation data provide loose contact-surface information. The usefulness of this method was demonstrated through the structure determination of the p62 PB1-PB1 complex, which forms a front-to-back 20 kDa homo-oligomer. As p62 PB1 does not intrinsically bind metal ions, the lanthanide binding peptide tag was attached to one subunit of the dimer at two anchoring points. Each monomer was treated as a rigid body and was docked based on the backbone PCS and backbone chemical shift perturbation data. Unlike NOE-based structural determination, this method only requires resonance assignments of the backbone (1)H(N)/(15)N signals and the PCS data obtained from several sets of two-dimensional (15)N-heteronuclear single quantum coherence spectra, thus facilitating rapid structure determination of the protein-protein complex.
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