1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid-induced protein 2

被引:4
作者
Lang, Andras [1 ]
Goradia, Nishit [2 ]
Wikman, Harriet [3 ]
Werner, Stefan [3 ]
Wilmanns, Matthias [2 ,4 ]
Ohlenschlaeger, Oliver [1 ]
机构
[1] Leibniz Inst Aging, Fritz Lipmann Inst, Beutenbergstr 11, D-07745 Jena, Germany
[2] European Mol Biol Lab, Hamburg Unit, Notkestr 85, D-22607 Hamburg, Germany
[3] Univ Med Ctr Hamburg Eppendorf, Inst Tumor Biol, Martinistr 52, D-20246 Hamburg, Germany
[4] Univ Med Ctr Hamburg Eppendorf, Martinistr 52, D-20246 Hamburg, Germany
关键词
Resonance assignments; Chemical shift; Heteronuclear NMR; Retinoic acid-induced protein 2; Tumor suppressor; NMR-SPECTROSCOPY;
D O I
10.1007/s12104-020-09960-9
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Retinoic acid-induced protein 2 is a human protein of 530 residues encoded by the RAI2 gene (Q9Y5P3; RAI2_HUMAN). RAI2 is a novel tumor suppressor protein whose depletion in breast cancer cell lines results in the downregulation of several genes associated with differentiation along with increased invasiveness and aggressive tumor phenotype of the cells. The role of the protein is specified to be a transcriptional regulator that promotes chromosomal stability and hence controls the expression of several regulators of cancer and metastasis. Structurally, RAI2 remains an unknown entity and, hence, to obtain a detailed view on the structure function relationship we report the(1)H,C-13, and(15)N resonance assignments for the backbone and side chain nuclei of the C-terminal region (a.a. 303-451 of UniProt Q9Y5P3) of RAI2.
引用
收藏
页码:271 / 275
页数:5
相关论文
共 16 条
[1]  
BAX A, 1991, Journal of Biomolecular NMR, V1, P99, DOI 10.1007/BF01874573
[2]   (H)N(COCA)NH and (HN)under-bar(COCA)NH experiments for H-1-N-15 backbone assignments in C-13/N-15-labeled proteins [J].
Bracken, C ;
Palmer, AG ;
Cavanagh, J .
JOURNAL OF BIOMOLECULAR NMR, 1997, 9 (01) :94-100
[3]   A CONSTANT-TIME 3-DIMENSIONAL TRIPLE-RESONANCE PULSE SCHEME TO CORRELATE INTRARESIDUE H-1(N), N-15, AND C-13(') CHEMICAL-SHIFTS IN N-15-C-13-LABELED PROTEINS [J].
CLUBB, RT ;
THANABAL, V ;
WAGNER, G .
JOURNAL OF MAGNETIC RESONANCE, 1992, 97 (01) :213-217
[4]  
Erdos Gabor, 2020, Curr Protoc Bioinformatics, V70, pe99, DOI 10.1002/cpbi.99
[5]  
GRZESIEK S, 1993, J BIOMOL NMR, V3, P185
[6]   Combined automated NOE assignment and structure calculation with CYANA [J].
Guentert, Peter ;
Buchner, Lena .
JOURNAL OF BIOMOLECULAR NMR, 2015, 62 (04) :453-471
[7]   CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts [J].
Hafsa, Noor E. ;
Arndt, David ;
Wishart, David S. .
NUCLEIC ACIDS RESEARCH, 2015, 43 (W1) :W370-W377
[8]   3-DIMENSIONAL TRIPLE-RESONANCE NMR-SPECTROSCOPY OF ISOTOPICALLY ENRICHED PROTEINS [J].
KAY, LE ;
IKURA, M ;
TSCHUDIN, R ;
BAX, A .
JOURNAL OF MAGNETIC RESONANCE, 1990, 89 (03) :496-514
[9]  
Keller RLJ, 2004, COMPUTER AIDED RESON
[10]   OVERCOMING THE OVERLAP PROBLEM IN THE ASSIGNMENT OF H-1-NMR SPECTRA OF LARGER PROTEINS BY USE OF 3-DIMENSIONAL HETERONUCLEAR H-1-N-15 HARTMANN-HAHN MULTIPLE QUANTUM COHERENCE AND NUCLEAR OVERHAUSER MULTIPLE QUANTUM COHERENCE SPECTROSCOPY - APPLICATION TO INTERLEUKIN-1-BETA [J].
MARION, D ;
DRISCOLL, PC ;
KAY, LE ;
WINGFIELD, PT ;
BAX, A ;
GRONENBORN, AM ;
CLORE, GM .
BIOCHEMISTRY, 1989, 28 (15) :6150-6156