Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered

被引:0
作者
Wiedemann, Christoph [1 ,4 ]
Obika, Kingsley Benjamin [1 ]
Liebscher, Sandra [1 ]
Jirschitzka, Jan [2 ]
Ohlenschlager, Oliver [3 ]
Bordusa, Frank [1 ]
机构
[1] Martin Luther Univ Halle Wittenberg, Charles Tanford Prot Ctr, Inst Biochem & Biotechnol, Kurt Mothes Str 3a, D-06120 Halle, Germany
[2] Univ Cologne, Inst Biochem, Dept Chem, Zulpicher Str 47, D-50674 Cologne, Germany
[3] Fritz Lipmann Inst, Leibniz Inst Aging, Beutenbergstr 11, D-07745 Jena, Germany
[4] Friedrich Schiller Univ Jena, Fac Chem & Earth Sci, Inst Organ Chem & Macromol Chem & Cluster Excelle, Biostruct Interact, Humboldtstr 10, D-07743 Jena, Germany
关键词
Nuclear magnetic resonance spectroscopy; NMR; Intrinsically disordered protein; IDP; Human protein; Resonance chemical shift assignment; Structural and functional; Uncharacterized human protein; NMR-SPECTROSCOPY; LARGER PROTEINS; SECONDARY STRUCTURE; C-13; SENSITIVITY; RESONANCES; AMIDE; N-15; PREDICTION; SPECTRA;
D O I
10.1007/s12104-021-10043-6
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Even though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these "unknown" proteins may help to identify possible cellular tasks. We therefore used a combination of bioinformatics and nuclear magnetic resonance spectroscopy to structurally de-orphanize one of these gene products, the 108 amino acid human uncharacterized protein CXorf51A. Both our bioinformatics analysis as well as the H-1, C-13, N-15 backbone and near-complete side-chain chemical shift assignments indicate that it is an intrinsically disordered protein.
引用
收藏
页码:441 / 448
页数:8
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