ArticleBiophysical journal2002
Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Solution structure and dynamics of the mitochondrial-targeted GTPase-activating protein (GAP) VopE by an integrated NMR/SAXS approach.Protein science : a publication of the Protein Society · 2022Article
- Determining Complex Structures using Docking Method with Single Particle Scattering Data.Frontiers in molecular biosciences · 2017Article
- Enzyme-linked DNA dendrimer nanosensors for acetylcholine.Scientific reports · 2015Article
- Combining NMR and small angle X-ray and neutron scattering in the structural analysis of a ternary protein-RNA complex.Journal of biomolecular NMR · 2013Article
- Sample preparation, data collection, and preliminary data analysis in biomolecular solution X-ray scattering.Current protocols in protein science · 2012Article
- A simple procedure to evaluate the efficiency of bio-macromolecular rigid-body refinement by small-angle scattering.European biophysics journal : EBJ · 2012Article
- Nuclear magnetic resonance analysis of protein-DNA interactions.Journal of the Royal Society, Interface · 2011Review
- Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.Biophysical journal · 2010Article
- A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation.The Journal of biological chemistry · 2010Article
- Structure and flexibility within proteins as identified through small angle X-ray scattering.General physiology and biophysics · 2009Article
- A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints.Journal of biomolecular NMR · 2008Article
- Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints.Journal of biomolecular NMR · 2008Article
- A simple genetic algorithm for the optimization of multidomain protein homology models driven by NMR residual dipolar coupling and small angle X-ray scattering data.European biophysics journal : EBJ · 2007Article
- Structural assembly of multidomain proteins and protein complexes guided by the overall rotational diffusion tensor.Journal of the American Chemical Society · 2007Article
- The structure of free L11 and functional dynamics of L11 in free, L11-rRNA(58 nt) binary and L11-rRNA(58 nt)-thiostrepton ternary complexes.Journal of molecular biology · 2007Article
- Joint use of small-angle X-ray and neutron scattering to study biological macromolecules in solution.European biophysics journal : EBJ · 2006Article
- A target function for quaternary structural refinement from small angle scattering and NMR orientational restraints.European biophysics journal : EBJ · 2006Article
- Global rigid body modeling of macromolecular complexes against small-angle scattering data.Biophysical journal · 2005Article
- Alignment of chain-like molecules.Journal of biomolecular NMR · 2004Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new principle in constructing molecular complexes from the known high-resolution domain structures joining data from NMR and small-angle x-ray scattering (SAXS) measurements is described. Structure of calmodulin in complex with trifluoperazine was built from N- and C-terminal domains oriented based on residual dipolar couplings measured by NMR in a dilute liquid crystal, and the overall shape of the complex was derived from SAXS data. The residual dipolar coupling data serves to reduce angular degrees of freedom, and the small-angle scattering data serves to confine the translational degrees of freedom. The complex built by this method was found to be consistent with the known crystal structure. The study demonstrates how approximate tertiary structures of modular proteins or quaternary structures composed of subunits can be assembled from high-resolution structures of domains or subunits using mutually complementary NMR and SAXS data.
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