Publication date: Available online 1 October 2013 Source:Methods
Author(s): Jaelle N. Foot , Mikael Feracci , Cyril Dominguez
In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory roles. Associated with that, the number of identified RNA binding proteins (RBP) has increased considerably and mutations in RNA molecules or RBP have been shown to cause various diseases, such as cancers. It is therefore crucial to understand at the molecular level how these proteins specifically recognize their RNA targets in order to design new generation drug therapies targeting protein-RNA complexes. Nuclear Magnetic Resonance (NMR) is a particularly well-suited technique to study such protein-RNA complexes at the atomic level and can provide valuable information for new drug discovery programs. In this chapter, we describe the NMR strategy that we and other laboratories use for screening optimal conditions necessary for structural studies of protein-single stranded RNA complexes, using two proteins, Sam68 and T-STAR, as examples.
Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy
Structure determination and dynamics of protein–RNA complexes by NMR spectroscopy
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 58, Issues 1–2</br>
Cyril Dominguez, Mario Schubert, Olivier Duss, Sapna Ravindranathan, Frédéric H.-T. Allain</br>
</br>
</br></br>
nmrlearner
Journal club
0
03-09-2012 09:16 AM
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
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
11-24-2010 09:25 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>
More...
nmrlearner
Journal club
0
10-07-2010 02:32 PM
[NMR paper] Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by N
Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Related Articles Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Biochemistry. 1995 Jan 10;34(1):148-54
Authors: Davis KG, Plyte SE, Robertson SR, Cooper A, Kneale GG
The Pf1 gene 5 protein forms a large helical nucleoprotein complex (Mr = 3.1 x 10(7)) with single-stranded viral DNA, from which a 32 amino acid...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] Secondary structure of the single-stranded DNA binding protein encoded by filamentous
Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
Eur J Biochem. 1994 Sep 1;224(2):663-76
Authors: Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW
Nuclear magnetic resonance...
nmrlearner
Journal club
0
08-22-2010 03:29 AM
[NMR paper] Identification of the single-stranded DNA binding surface of the transcriptional coac
Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
J Biol Chem. 1999 Feb 5;274(6):3693-9
Authors: Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R
The C-terminal domain of the eukaryotic transcriptional cofactor PC4...
nmrlearner
Journal club
0
08-21-2010 04:03 PM
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...