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The N- and C-termini of the human Nogo molecules are intrinsically unstructured: Bioinformatics, CD, NMR characterization, and functional implications by Minfen Li; Jianxing Song is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract RTN4 or Nogo proteins are composed of three alternative splice forms, namely 1192‐residue Nogo‐A, 373‐residue Nogo‐B, and 199‐residue Nogo‐C. Nogo proteins have received intense attentions because they have been implicated in a variety of critical cellular processes including CNS neuronal regeneration, vascular remodeling, apoptosis, interaction with β‐amyloid protein converting enzyme, and generation/maintenance of the tubular network of the endoplasmic reticulum (ER). Despite their significantly‐different N‐terminal lengths, they share a conserved C‐terminal reticulon‐homology domain consisting of two transmembrane fragments, a 66‐residue extracellular loop Nogo‐66 and a 38‐residue C‐tail carrying ER retention motif. Nogo‐A owns the largest N‐terminus with 1016 residues while the Nogo‐B has an N‐terminus almost identical to the first 200 residues of Nogo‐A. So far, except for our previous determination of the Nogo‐66 solution structure, no structural characterization of the other Nogo regions has been reported. In the present study, we initiated a systematically investigation of structural properties of Nogo molecules by a combined use of bioinformatics, CD, and NMR s

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Author

Minfen Li; Jianxing Song

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)