Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/15659
Title: Structural studies on DdCAD-1: A Ca2+-dependent cell-cell adhesion protein
Authors: LIN ZHI
Keywords: NMR, adhesion, Ca2+-dependent, DdCAD-1, aromatic assignment
Issue Date: 13-Dec-2006
Source: LIN ZHI (2006-12-13). Structural studies on DdCAD-1: A Ca2+-dependent cell-cell adhesion protein. ScholarBank@NUS Repository.
Abstract: DdCAD-1 is a novel Ca2+-dependent cell adhesion molecule from Dictyostelium discoideum. In this study, we described the novel features of the NMR structures of Ca2+-free and Ca2+-bound DdCAD-1 in monomeric forms based on multi-dimensional NMR spectroscopy. DdCAD-1 contains two i??-sandwich domains, resembling I?I?a??crystallins and cadherins, respectively. Distinct binding interactions are ascribed for the two domains of DdCAD-1. Based on structural and mutagenesis analyses, we proposed a model for the Ca2+-bound DdCAD-1 dimer as a basis for understanding DdCAD-1-mediated cell-cell adhesion. Our results provide new insights into Ca2+-dependent mechanism for cell-cell adhesion. In addition, we developed a new strategy for the assignment of aromatic side-chain resonances of 13C, 15N-labeled proteins. The aromatic assignment can be achieved using a single 3D 13C- and 15N-edited NOESY experiment on the basis of prior assignment of backbone and aliphatic side-chain resonances. This strategy can improve the precision of protein structures, especially for large proteins.
URI: http://scholarbank.nus.edu.sg/handle/10635/15659
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