2g31
From Proteopedia
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Human Nogo-A functional domain: nogo60
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Schizophrenia, susceptibility to OMIM:[605566]
About this Structure
2G31 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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., Li M, Liu J, Song J, Protein Sci. 2006 Aug;15(8):1835-41. PMID:16877707
Page seeded by OCA on Mon Nov 12 22:13:58 2007
Categories: Homo sapiens | Single protein | Li, M.F. | Liu, J.X. | Song, J.X. | Helix | Nogo
