NMR solution structure determination of large RNA-protein
complexes

J 2016

NMR solution structure determination of large RNA-protein complexes

YADAV, Deepak Kumar a Peter LUKAVSKY

Základní údaje

Originální název

NMR solution structure determination of large RNA-protein complexes

Autoři

YADAV, Deepak Kumar (356 Indie, domácí) a Peter LUKAVSKY (40 Rakousko, garant, domácí)

Vydání

PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, OXFORD, PERGAMON-ELSEVIER SCIENCE LTD, 2016, 0079-6565

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10403 Physical chemistry

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.971

Kód RIV

RIV/00216224:14740/16:00088765

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.pnmrs.2016.10.001

UT WoS

000390507100003

Klíčová slova anglicky

Biomolecular NMR; RNA-protein complex; NMR assignments; NMR structure determination; RNA-protein interaction; Isotope labeling; Integrated structural biology

Štítky

CF NMR, rivok

Změněno: 10. 3. 2017 09:39, Mgr. Eva Špillingová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

EE2.3.20.0042, projekt VaV

Název: Internacionalizace programu Strukturní biologie s důrazem na rozvoj nových směrů výzkumu

GA15-21122S, projekt VaV

Název: Strukturní podstata změn v sestřihu způsobující cystickou fibrózu

Investor: Grantová agentura ČR, Strukturní podstata změn v sestřihu způsobující cystickou fibrózu

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

YADAV, Deepak Kumar a Peter LUKAVSKY. NMR solution structure determination of large RNA-protein complexes. PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY. OXFORD: PERGAMON-ELSEVIER SCIENCE LTD, 2016, roč. 97, November, s. 57-81. ISSN 0079-6565. Dostupné z: https://dx.doi.org/10.1016/j.pnmrs.2016.10.001.

@article{1375140,
   author = {Yadav, Deepak Kumar and Lukavsky, Peter},
   article_location = {OXFORD},
   article_number = {November},
   doi = {http://dx.doi.org/10.1016/j.pnmrs.2016.10.001},
   keywords = {Biomolecular NMR; RNA-protein complex; NMR assignments; NMR structure determination; RNA-protein interaction; Isotope labeling; Integrated structural biology},
   language = {eng},
   issn = {0079-6565},
   journal = {PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY},
   title = {NMR solution structure determination of large RNA-protein complexes},
   url = {http://www.sciencedirect.com/science/article/pii/S0079656516300310},
   volume = {97},
   year = {2016}
}

TY  - JOUR
ID  - 1375140
AU  - Yadav, Deepak Kumar - Lukavsky, Peter
PY  - 2016
TI  - NMR solution structure determination of large RNA-protein complexes
JF  - PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
VL  - 97
IS  - November
SP  - 57-81
EP  - 57-81
PB  - PERGAMON-ELSEVIER SCIENCE LTD
SN  - 00796565
KW  - Biomolecular NMR
KW  - RNA-protein complex
KW  - NMR assignments
KW  - NMR structure determination
KW  - RNA-protein interaction
KW  - Isotope labeling
KW  - Integrated structural biology
UR  - http://www.sciencedirect.com/science/article/pii/S0079656516300310
L2  - http://www.sciencedirect.com/science/article/pii/S0079656516300310
N2  - 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.
ER  -

YADAV, Deepak Kumar a Peter LUKAVSKY. NMR solution structure determination of large RNA-protein complexes. \textit{PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY}. OXFORD: PERGAMON-ELSEVIER SCIENCE LTD, 2016, roč.~97, November, s.~57-81. ISSN~0079-6565. Dostupné z: https://dx.doi.org/10.1016/j.pnmrs.2016.10.001.

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