NMR solution structure determination of large RNA-protein complexes

Investor logo
Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Medicine. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.

Authors

YADAV Deepak Kumar LUKAVSKY Peter

Year of publication 2016
Type Article in Periodical
Magazine / Source PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.sciencedirect.com/science/article/pii/S0079656516300310
Doi http://dx.doi.org/10.1016/j.pnmrs.2016.10.001
Field Physical chemistry and theoretical chemistry
Keywords Biomolecular NMR; RNA-protein complex; NMR assignments; NMR structure determination; RNA-protein interaction; Isotope labeling; Integrated structural biology
Description Structure determination of RNA-protein complexes is essential for our understanding of the multiple layers of RNA-mediated posttranscriptional regulation of gene expression. Over the past 20 years, NMR spectroscopy became a key tool for structural studies of RNA-protein interactions. Here, we review the progress being made in NMR structure determination of large ribonucleoprotein assemblies. We discuss approaches for the design of RNA-protein complexes for NMR structural studies, established and emerging isotope and segmental labeling schemes suitable for large RNPs and how to gain distance restraints from NOEs, PREs and EPR and orientational information from RDCs and SAXS/SANS in such systems. the new combination of NMR measurements with MD simulations and its potential will also be discussed. Application and combination of these various methods for structure determination of large RNPs will be illustrated with three large RNA-protein complexes (>40 kDa) and other interesting complexes determined in the past six and a half years. (C) 2016 Elsevier B.V. All rights reserved.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info