La-related protein 7 (LARP7) are a family of RNA chaperones that protect the 3'-end of RNA and are components of specific ribonucleoprotein complexes (RNP). In Tetrahymena thermophila telomerase, LARP7 protein p65 together with telomerase reverse transcriptase (TERT) and telomerase RNA (TER) form the core RNP. p65 has four known domains-N-terminal domain (NTD), La motif (LaM), RNA recognition motif 1 (RRM1), and C-terminal xRRM2. To date, only the xRRM2 and LaM and their interactions with TER...
[NMR paper] NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
Related Articles NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase.
Biomol NMR Assign. 2015 Dec 31;
Authors: Polshakov VI, Petrova OA, Parfenova YY, Efimov SV, Klochkov VV, Zvereva MI, Dontsova OA
Abstract
Telomerase is a ribonucleoprotein enzyme that adds telomeric DNA fragments to the ends of chromosomes. This enzyme is the focus of substantial attention, both because its structure and...
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01-03-2016 01:25 AM
De novo protein structure determination from near-atomic-resolution cryo-EM maps - Nature.com
De novo protein structure determination from near-atomic-resolution cryo-EM maps - Nature.com
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De novo protein structure determination from near-atomic-resolution cryo-EM maps
Nature.com
Despite these developments, little progress has been made in de novo model building into near-atomic-resolution cryo-EM density maps. Structural interpretation of cryo-EM maps typically starts with fitting an atomic X-ray or NMR structure into the map5.
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[NMR paper] Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Apr 29;
Authors: Scanu S, Förster J, Ullmann GM, Ubbink M
Abstract
Protein complex formation is thought to be at least a two-step process, in which the active complex is preceded by the formation of an encounter complex....
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05-01-2013 11:46 AM
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.
Proc Natl Acad Sci U S A. 2011 Jul 5;
Authors: Kato H, van Ingen H, Zhou BR, Feng H, Bustin M, Kay LE, Bai Y
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility...
Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR
Linear Mode
