Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2007.06.031
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dc.titleNogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain
dc.contributor.authorLi, M.
dc.contributor.authorSong, J.
dc.date.accessioned2011-11-29T06:10:34Z
dc.date.available2011-11-29T06:10:34Z
dc.date.issued2007
dc.identifier.citationLi, 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.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/28882
dc.description.abstractRTN4/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.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbrc.2007.06.031
dc.sourceScopus
dc.subjectBioinformatics
dc.subjectCD spectroscopy
dc.subjectIntrinsically unstructured
dc.subjectNMR spectroscopy
dc.subjectNogo proteins
dc.subjectNogo-B receptor
dc.subjectPartially folded
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.bbrc.2007.06.031
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume360
dc.description.issue1
dc.description.page128-134
dc.description.codenBBRCA
dc.identifier.isiut000248137400021
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