2g31: Difference between revisions
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[[Image:2g31.gif|left|200px]] | [[Image:2g31.gif|left|200px]] | ||
'''Human Nogo-A functional domain: nogo60''' | {{Structure | ||
|PDB= 2g31 |SIZE=350|CAPTION= <scene name='initialview01'>2g31</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= NOGO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Human Nogo-A functional domain: nogo60''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2G31 is a [ | 2G31 is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16877707 16877707] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nogo]] | [[Category: nogo]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:59:46 2008'' | ||
Revision as of 14:59, 20 March 2008
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| 2g31 | |||||||||||||
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| Gene: | NOGO (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Human Nogo-A functional domain: nogo60
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 Mar 20 16:59:46 2008
