Related ArticlesStructure determination of protein/RNA complexes by NMR.
Methods Enzymol. 2005;394:525-45
Authors: Wu H, Finger LD, Feigon J
Structure determination of protein?RNA complexes in solution provides unique insights into factors that are involved in protein/RNA recognition. Here, we review the methodology used in our laboratory to overcome the challenges of protein?RNA structure determination by nuclear magnetic resonance (NMR). We use as two examples complexes recently solved in our laboratory, the nucleolin RBD12/b2NRE and Rnt1p dsRBD/snR47h complexes. Topics covered are protein and RNA preparation, complex formation, identification of the protein/RNA interface, protein and RNA resonance assignment, intermolecular NOE assignment, and structure calculation and analysis.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Methods Enzymol. 2011;493:241-75
Authors: Ziarek JJ, Peterson FC, Lytle BL, Volkman BF
Over the last 15years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like...
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03-05-2011 01:02 PM
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Prog Nucl Magn Reson Spectrosc. 2011 Feb;58(1-2):1-61
Authors: Dominguez C, Schubert M, Duss O, Ravindranathan S, Allain FH
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01-19-2011 11:18 AM
[NMR paper] Structure determination of protein complexes by NMR.
Structure determination of protein complexes by NMR.
Related Articles Structure determination of protein complexes by NMR.
Methods Mol Biol. 2004;278:255-88
Authors: Nietlispach D, Mott HR, Stott KM, Nielsen PR, Thiru A, Laue ED
This chapter describes nuclear magnetic resonance (NMR) methods that can be used to determine the structures of protein complexes. Many of these techniques are also applicable to other systems (e.g., protein-nucleic acid complexes). In the first section, we discuss methodologies for optimizing the sample conditions for...
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11-24-2010 09:25 PM
[NMR paper] NMR structure determination of proteins and protein complexes larger than 20 kDa.
NMR structure determination of proteins and protein complexes larger than 20 kDa.
Related Articles NMR structure determination of proteins and protein complexes larger than 20 kDa.
Curr Opin Chem Biol. 1998 Oct;2(5):564-70
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional nuclear magnetic resonance methodology to obtain 1H, 15N and 13C resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long-range order, coupled with new methods of structure refinement and novel methods...
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11-17-2010 11:15 PM
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 6 October 2010</br>
Cyril, Dominguez , Mario, Schubert , Olivier, Duss , Sapna, Ravindranathan , Frédéric H.-T., Allain</br>
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10-07-2010 02:32 PM
PCS-based structure determination of proteinâ??protein complexes
Abstract A simple and fast nuclear magnetic resonance method for docking proteins using pseudo-contact shift (PCS) and 1HN/15N 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 (~40 Ã?) distance and angular restraints between the lanthanide ion and the observed nuclei, while the 1HN/15N chemical shift perturbation data provide loose contact-surface information. The usefulness of this method was demonstrated through the structure...
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08-14-2010 04:19 AM
Structure Determination of Protein Complexes by NMR
Structure Determination of Protein Complexes by NMR
D. Nietlispach, H.R. Mott, K.M. Stott, P.R. Nielsen, A. Thiru & E.D. Laue
The Department of Biochemistry, University of Cambridge
Introduction
As the structures of more proteins and domains are solved by structural genomics projects, the future of structural biology will be oriented more toward the study of macromolecular complexes. Since so many biological processes are mediated by interactions between proteins, it is important to study them at a molecular level. The study of protein-protein interactions also has applications in a...
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08-29-2008 02:43 AM
Structure Determination of Protein-Ligand Complexes by Transferred Paramagnetic Shifts
Structure Determination of Protein-Ligand Complexes by Transferred Paramagnetic Shifts
Michael John, Guido Pintacuda, Ah Young Park, Nicholas E. Dixon, and Gottfried Otting
J. Am. Chem. Soc.; 2006; 128(39) pp 12910 - 12916; (Article)
Abstract:
Rational drug design depends on the knowledge of the three-dimensional (3D) structure of complexes between proteins and lead compounds of low molecular weight. A novel nuclear magnetic resonance (NMR) spectroscopy strategy based on the paramagnetic effects from lanthanide ions allows the rapid determination of the 3D structure of a small...