2g31
From Proteopedia
(New page: 200px<br /> <applet load="2g31" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g31" /> '''Human Nogo-A functional domain: nogo60'''<b...) |
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'''Human Nogo-A functional domain: nogo60'''<br /> | '''Human Nogo-A functional domain: nogo60'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The inability to determine the structure of the buffer-insoluble Nogo | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2G31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2G31 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G31 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Li, M | + | [[Category: Li, M F.]] |
| - | [[Category: Liu, J | + | [[Category: Liu, J X.]] |
| - | [[Category: Song, J | + | [[Category: Song, J X.]] |
[[Category: helix]] | [[Category: helix]] | ||
[[Category: nogo]] | [[Category: nogo]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:37 2008'' |
Revision as of 15:27, 21 February 2008
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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 Thu Feb 21 17:27:37 2008
Categories: Homo sapiens | Single protein | Li, M F. | Liu, J X. | Song, J X. | Helix | Nogo
