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1H, 13C, 15N backbone and side-chain resonance assignments of the human Raf-1 kinase inhibitor protein

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Abstract

Raf-1 kinase inhibitor protein (RKIP) plays a pivotal role in modulating multiple signaling networks. Here we report backbone and side chain resonance assignments of uniformly 15N, 13C labeled human RKIP.

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References

  • Banfield MJ, Barker JJ et al (1998) Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure 6(10):1245–1254

    Article  Google Scholar 

  • Corbit KC, Trakul N et al (2003) Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J Biol Chem 278(15):13061–13068

    Article  Google Scholar 

  • Delaglio F, Grzesiek S et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293

    Article  Google Scholar 

  • Dhillon AS, Hagan S et al (2007) MAP kinase signalling pathways in cancer. Oncogene 26(22):3279–3290

    Article  Google Scholar 

  • Frayne J, McMillen A et al (1998) Expression of phosphatidylethanolamine-binding protein in the male reproductive tract: immunolocalisation and expression in prepubertal and adult rat testes and epididymides. Mol Reprod Dev 49(4):454–460

    Article  Google Scholar 

  • Frayne J, Ingram C et al (1999) Localisation of phosphatidylethanolamine-binding protein in the brain and other tissues of the rat. Cell Tissue Res 298(3):415–423

    Article  Google Scholar 

  • Kroslak T, Koch T et al (2001) Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling. J Biol Chem 276(43):39772–39778

    Article  Google Scholar 

  • Lorenz K, Lohse MJ et al (2003) Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2. Nature 426(6966):574–579

    Article  ADS  Google Scholar 

  • Pearson G, Robinson F et al (2001) Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr Rev 22(2):153–183

    Article  Google Scholar 

  • Roberts PJ, Der CJ (2007) Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene 26(22):3291–3310

    Article  Google Scholar 

  • Schoentgen F, Seddiqi N et al (1992) Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated through hydrophobic cluster analysis and molecular modelling. Protein Eng 5(4):295–303

    Article  Google Scholar 

  • Trakul N, Rosner MR (2005) Modulation of the MAP kinase signaling cascade by Raf kinase inhibitory protein. Cell Res 15(1):19–23

    Article  Google Scholar 

  • Wellbrock C, Karasarides M et al (2004) The RAF proteins take centre stage. Nat Rev Mol Cell Biol 5(11):875–885

    Article  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4(2):171–180

    Article  Google Scholar 

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Acknowledgments

This work was supported by grants from the Natural Science Foundation of China (Nos. 30900233, 30730026) and the Program of Shanghai Subject Chief Scientist (No. 09XD1405100). We would like to thank Prof. J. Y. Li for providing the human RKIP gene.

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Correspondence to Donghai Lin.

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Yi, C., Peng, Y., Guo, C. et al. 1H, 13C, 15N backbone and side-chain resonance assignments of the human Raf-1 kinase inhibitor protein. Biomol NMR Assign 5, 63–66 (2011). https://doi.org/10.1007/s12104-010-9268-z

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  • DOI: https://doi.org/10.1007/s12104-010-9268-z

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