ArticleJournal of the American Chemical Society2009
Determination of multicomponent protein structures in solution using global orientation and shape restraints.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Review
- Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS.Biophysical journal · 2021Article
- Modeling and Structure Determination of Homo-Oligomeric Proteins: An Overview of Challenges and Current Approaches.International journal of molecular sciences · 2021Review
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Article
- Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.Journal of biomolecular NMR · 2019Article
- Using Small-Angle Scattering Data and Parametric Machine Learning to Optimize Force Field Parameters for Intrinsically Disordered Proteins.Frontiers in molecular biosciences · 2019Article
- Methods for SAXS-based structure determination of biomolecular complexes.Advanced materials (Deerfield Beach, Fla.) · 2014Article
- Structural characterization of a flexible two-domain protein in solution using small angle X-ray scattering and NMR data.Structure (London, England : 1993) · 2014Article
- The dynamic duo: combining NMR and small angle scattering in structural biology.Protein science : a publication of the Protein Society · 2014Review
- Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.Protein science : a publication of the Protein Society · 2014Article
- Multiple conformations of SAM-II riboswitch detected with SAXS and NMR spectroscopy.Nucleic acids research · 2012Article
- A simple procedure to evaluate the efficiency of bio-macromolecular rigid-body refinement by small-angle scattering.European biophysics journal : EBJ · 2012Article
- High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.Journal of biomolecular NMR · 2011Article
- Nuclear magnetic resonance analysis of protein-DNA interactions.Journal of the Royal Society, Interface · 2011Review
- Structural NMR of protein oligomers using hybrid methods.Journal of structural biology · 2011Review
- Crystallographic and nuclear magnetic resonance evaluation of the impact of peptide binding to the second PDZ domain of protein tyrosine phosphatase 1E.Biochemistry · 2010Article
- Rapid global structure determination of large RNA and RNA complexes using NMR and small-angle X-ray scattering.Methods (San Diego, Calif.) · 2010Review
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12 authors.
Funding
Abstract
Determining architectures of multicomponent proteins or protein complexes in solution is a challenging problem. Here we report a methodology that simultaneously uses residual dipolar couplings (RDC) and the small-angle X-ray scattering (SAXS) restraints to mutually orient subunits and define the global shape of multicomponent proteins and protein complexes. Our methodology is implemented in an efficient algorithm and demonstrated using five examples. First, we demonstrate the general approach with simulated data for the HIV-1 protease, a globular homodimeric protein. Second, we use experimental data to determine the structures of the two-domain proteins L11 and gammaD-Crystallin, in which the linkers between the domains are relatively rigid. Finally, complexes with K(d) values in the high micro- to millimolar range (weakly associating proteins), such as a homodimeric GB1 variant, and with K(d) values in the nanomolar range (tightly bound), such as the heterodimeric complex of the ILK ankyrin repeat domain (ARD) and PINCH LIM1 domain, respectively, are evaluated. Furthermore, the proteins or protein complexes that were determined using this method exhibit better solution structures than those obtained by either NMR or X-ray crystallography alone as judged based on the pair-distance distribution functions (PDDF) calculated from experimental SAXS data and back-calculated from the structures.
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