1H, 13C and 15N NMR chemical shift assignments of A-thaliana RCD1 RST

被引：6
|
作者：
Tossavainen, Helena [1 ]
Hellman, Maarit [2 ]
Vainonen, Julia P. [3 ]
Kangasjarvi, Jaakko [3 ]
Permi, Perttu [1 ,2 ,4 ]
机构：
[1] Univ Helsinki, Inst Biotechnol, Program Struct Biol & Biophys, Helsinki, Finland
[2] Univ Jyvaskyla, Dept Chem, Nanosci Ctr, Jyvaskyla, Finland
[3] Univ Helsinki, Div Plant Biol, Dept Biosci, Viikki Plant Sci Ctr, Helsinki, Finland
[4] Univ Jyvaskyla, Dept Biol & Environm Sci, Nanosci Ctr, Jyvaskyla, Finland
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2017年 / 11卷 / 02期
基金：
芬兰科学院;
关键词：
NMR assignments; RCD1; RST; INTRINSICALLY DISORDERED PROTEINS;
D O I：
10.1007/s12104-017-9749-4
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The A. thaliana RCD1 (radical-induced cell death1) protein is a cellular signaling hub protein which interacts with numerous plant transcription factors from different families. It consists of three conserved domains and intervening unstructured regions, the C-terminal RST domain being responsible for the interactions with the transcription factors. It has been shown that many partner proteins interact with RCD1 RST via their intrinsically disordered regions, and that the domain is able to house partners with divergent folds. We aim to structurally characterize the RCD1 RST domain and its complexes [complex with DREB2A]. Here we report the H-1, N-15 and C-13 chemical shift assignments of the backbone and sidechain atoms for RCD1 (468-589) containing the RST (510-567) domain.
引用
收藏
页码：207 / 210
页数：4
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