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Protein Science (2006), 15:1835-1841. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Nogo goes in the pure water: Solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration

Minfen Li1, Jingxian Liu2 and Jianxing Song1,2

1 Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore 119260, Singapore
2 Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 119260, Singapore

(RECEIVED April 25, 2006; FINAL REVISION May 16, 2006; ACCEPTED May 16, 2006)

The inability to determine the structure of the buffer-insoluble Nogo extracellular domain retarded further design of Nogo receptor (NgR) antagonists to treat CNS axonal injuries. Very surprisingly, we recently discovered that Nogo-60 was soluble and structured in salt-free water, thus allowing the determination of the first Nogo structure by heteronuclear NMR spectroscopy. Nogo-60 adopts an unusual helical structure with the N- and C-terminal helices connected by a long middle helix. While the N-helix has no contact with the rest of the molecule, the C-helix flips back to pack against the 20-residue middle helix. This packing appears to trigger the formation of the stable Nogo-60 structure because Nogo-40 with the last helix truncated is unstructured. The Nogo-60 structure offered us rationales for further design of the structured and buffer-soluble Nogo-54, which may be used as a novel NgR antagonist. Furthermore, our discovery may imply a general solution to solubilizing a category of buffer-insoluble proteins for urgent structural investigations.

Keywords: CNS injury; Nogo; Nogo-66 receptor; NMR spectroscopy; water; solution structure; protein solubility; protein folding


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M. Li, J. Liu, X. Ran, M. Fang, J. Shi, H. Qin, J.-M. Goh, and J. Song
Resurrecting Abandoned Proteins with Pure Water: CD and NMR Studies of Protein Fragments Solubilized in Salt-Free Water
Biophys. J., December 1, 2006; 91(11): 4201 - 4209.
[Abstract] [Full Text] [PDF]


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