(1)H, (13)C and (15)N NMR chemical shift assignments of A. thaliana RCD1 RST.
Related Articles (1)H, (13)C and (15)N NMR chemical shift assignments of A. thaliana RCD1 RST.
Biomol NMR Assign. 2017 Jun 07;:
Authors: Tossavainen H, Hellman M, Vainonen JP, Kangasjärvi J, Permi P
Abstract
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 (1)H, (15)N and (13)C chemical shift assignments of the backbone and sidechain atoms for RCD1 (468-589) containing the RST (510-567) domain.
PMID: 28593560 [PubMed - as supplied by publisher]
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