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|Title:||Structural characterization of nogo proteins: Implications for biological functions and moleculedesign of therapeutic applications||Authors:||LI MINFEN||Keywords:||Nogo, NMR spectroscopy, intrinsically unstructured, buffer-insoluble Nogo-60, buffer-soluble Nogo-54, protein solubility||Issue Date:||14-Dec-2007||Citation:||LI MINFEN (2007-12-14). Structural characterization of nogo proteins: Implications for biological functions and moleculedesign of therapeutic applications. ScholarBank@NUS Repository.||Abstract:||Nogos 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 o o Co and formation/maintenance of the tubular network of ER. In this study, we initiated a systematic NMR characterization of Nogo proteins. Firstly, the determination of the solution structure of the buffer-insoluble Nogo-60 offered us rationales to successfully design structured and buffer-soluble Nogo-54, which can be used as a template to further design novel NgR antagonists. Secondly, bioinformatics, CD and NMR characterization revealed that except for the Nogo66 loop, both N- and C-termini of Nogos were intrinsically-unstructured. Being intrinsically unstructured may allows Nogos to be involved in either cellular signaling processes or forming/maintaining membrane-related structures. In addition, we characterized the structural property of Nogo-B receptor and also identified a novel peptide of Nogo-A (171-181) with tight binding affinity with the third Nck2 SH3 domain.||URI:||http://scholarbank.nus.edu.sg/handle/10635/13102|
|Appears in Collections:||Ph.D Theses (Open)|
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