Please use this identifier to cite or link to this item:
|dc.title||Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain|
|dc.identifier.citation||Li, M., Song, J. (2007). Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. Biochemical and Biophysical Research Communications 360 (1) : 128-134. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2007.06.031|
|dc.description.abstract||RTN4/Nogo proteins containing three isoforms have been implicated in a large and diverse spectrum of biological functions. By contrast, only two functional receptors were known for them, namely NgR binding the 66-residue ectodomain shared by all three Nogos and NgBR specifically binding Nogo-B. The 297-residue NgBR was recently identified to be essential for stimulating chemotaxis and morphogenesis of endothelial cells but its structural property still remains completely unknown. In the present study, we expressed and subsequently conducted bioinformatics, CD and NMR characterization of NgBR and its two dissected domains. Very surprisingly, our results indicate that the NgBR ectodomain is intrinsically unstructured without both secondary and tertiary structures while the cytoplasmic domain is only partially folded with secondary structures but without a tight tertiary packing. Therefore, NgBR is a very rare example showing that the entire ectodomain of a transmembrane receptor could be predominantly disordered and the results presented here may bear important implications in understanding NgBR functions in the future. © 2007 Elsevier Inc. All rights reserved.|
|dc.description.sourcetitle||Biochemical and Biophysical Research Communications|
|Appears in Collections:||Staff Publications|
Show simple item record
Files in This Item:
There are no files associated with this item.
checked on May 20, 2019
WEB OF SCIENCETM
checked on May 13, 2019
checked on May 12, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.