Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/15890
Title: NMR study of the human NCK2 SH3 domains: Structure determination, binding diversity, folding and amyloidogenesis
Authors: LIU JINGXIAN
Keywords: NMR, SH3, NCK2, BINDING DIVERSITY, PROTEIN FOLDING, AMYLOIDOGENESIS
Issue Date: 4-Jun-2009
Source: LIU JINGXIAN (2009-06-04). NMR study of the human NCK2 SH3 domains: Structure determination, binding diversity, folding and amyloidogenesis. ScholarBank@NUS Repository.
Abstract: Nck2 contains three SH3 domains which are responsible for recruiting various effectors controlling cytoskeletonal dynamics and remodeling. The main objectives of the project are to determine structures, dynamics, binding specificities, folding properties and amyloidogenesis of Nck2 SH3 domains by use of NMR spectroscopy and other biophysical methods. Firstly, the NMR structures of two SH3 domains were successfully determined and the molecular mechanism for their binding to numerous peptides was defined. Secondly, the NMR evidence was obtained to show that a non-native helical conformation was highly-populated in a partially-folded SH3 domain. Moreover, a 4-residue region was identified to be critical for transforming the helical state to all-beta native state. Thirdly, the mechanism for amyloidogenesis of SH3 mutants was investigated. This study not only sheds light on the structural basis for Nck2-involved signaling pathways, but also contributes to our fundamental understanding of protein folding and amyloidogenesis underlying human neurodegenerative diseases.
URI: http://scholarbank.nus.edu.sg/handle/10635/15890
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