Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3.
Backbone and Ile, Leu, Val methyl group resonance assignment of CoV-Y domain of SARS-CoV-2 non-structural protein 3.
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DOI:
10.1007/s12104-021-10059-y
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发表时间:
2022-04
影响因子:
0.9
通讯作者:
Hoch JC
中科院分区:
文献类型:
--
作者:
Pustovalova Y;Gorbatyuk O;Li Y;Hao B;Hoch JC
The worldwide COVID-19 pandemic is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Nonstructural protein 3 (nsp3) has 1945 residues and is the largest protein encoded by SARS-CoV-2. It comprises more than a dozen independent domains with various functions. Many of these domains were studied in the closely-related virus SARS-CoV following an earlier outbreak. Nonetheless structural and functional information on the C-terminal region of nsp3 containing two transmembrane and three extra-membrane domains remains incomplete. This part of the protein appears to be involved in initiation of double membrane vesicle (DMV) formation, membranous organelles the virus builds to hide its replication-transcription complex from host immune defenses. Here we present the near-complete backbone and Ile, Leu, and Val methyl group chemical shift assignments of the most C-terminal domain of nsp3, CoV-Y. As the exact function and binding partners of CoV-Y remain unknown, our data provide a basis for future NMR studies of protein–protein interactions to elucidate the molecular mechanism of DMV formation.
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影响因子:
5
作者:
Imbert I;Snijder EJ;Dimitrova M;Guillemot JC;Lécine P;Canard B
通讯作者:
Canard B
影响因子:
2.9
作者:
Vranken, WF;Boucher, W;Laue, ED
通讯作者:
Laue, ED
影响因子:
6.4
作者:
Angelini MM;Akhlaghpour M;Neuman BW;Buchmeier MJ
通讯作者:
Buchmeier MJ
DOI:
10.1126/science.abd3629
发表时间:
2020-09-11
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Wolff G;Limpens RWAL;Zevenhoven-Dobbe JC;Laugks U;Zheng S;de Jong AWM;Koning RI;Agard DA;Grünewald K;Koster AJ;Snijder EJ;Bárcena M
通讯作者:
Bárcena M
影响因子:
2.7
作者:
DELAGLIO, F;GRZESIEK, S;BAX, A
通讯作者:
BAX, A