2G31

Human Nogo-A functional domain: nogo60

Summary for 2G31

• Entry DOI: 10.2210/pdb2g31/pdb
• NMR Information: BMRB: 7067
• Descriptor: Reticulon-4 (1 entity in total)
• Functional Keywords: nogo, helix, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: Q9NQC3
• Total number of polymer chains: 1
• Total formula weight: 6888.81

Authors

Li, M.F.,Liu, J.X.,Song, J.X. (deposition date: 2006-02-17, release date: 2006-08-22, Last modification date: 2024-05-29)

Primary citation

Li, M.F.,Liu, J.X.,Song, J.X.
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
Protein Sci., 15:1835-1841, 2006

PubMed Abstract: 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.

PubMed: 16877707
DOI: 10.1110/ps.062306906

Experimental method

SOLUTION NMR