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Letter to the editor: H-1, C-13 and N-15 resonance assignments of domain 1 of receptor associated protein

  1. Author:
    Wu, Y. B.
    Migliorini, M.
    Yu, P.
    Strickl, D. K.
    Wang, Y. X.

  2. Author Address

    Amer Red Cross, Jerome H Holland Lab Biomed Sci, Dept Vasc Biol, Rockville, MD 20855 USA Amer Red Cross, Jerome H Holland Lab Biomed Sci, Dept Vasc Biol, Rockville, MD 20855 USA NCI, Prot Nucleic Acid NMR Sect, Struct Biophys Lab, NIH, Frederick, MD 21702 USA Strickland DK Amer Red Cross, Jerome H Holland Lab Biomed Sci, Dept Vasc Biol, Rockville, MD 20855 USA
    1. Year: 2003
  2. Journal: Journal of Biomolecular Nmr
    1. 26
    2. 2
    3. Pages: 187-188
  4. Type of Article: Article
  1. Abstract:

    The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the H-1, C-13 and N- 15 chemical shift signals of domain 1 of the RAP.

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