Abstract
The serine-arginine rich family of proteins play important roles in the regulation of both constitutive and alternative splicing. SC35 (also known as SFRS2 and PR264) is a member of this family and contains one RNA recognition motif (RRM domain) and a RS domain at the C-terminus which is enriched with arginine and serine residues. SC35 is specifically involved in major regulatory pathways for cell proliferation and cell cycle progression. Determining the structure of SC35 would enable greater understanding of how its structure relates to its many functions. Complete 1H, 13C and 15N assignments of the RRM domain of SC35 are presented. The assignments were obtained using 2D heteronuclear and 3D triple-resonance experiments with the uniformly [15N,13C]-labelled protein. The chemical shifts are used to predict the 3-dimensional structure of this RRM domain in the absence of RNA.
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Acknowledgments
This study was supported by a grant from the BBSRC to J.C.C. and M.P. (grant number BB/D012716/1). The University of Liverpool is thanked for its support of the NMR Centre for Structural Biology.
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Clayton, J.C., Phelan, M., Goult, B.T. et al. The 1H, 13C and 15N backbone and side-chain assignment of the RRM domain of SC35, a regulator of pre-mRNA splicing. Biomol NMR Assign 5, 7–10 (2011). https://doi.org/10.1007/s12104-010-9254-5
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DOI: https://doi.org/10.1007/s12104-010-9254-5