Please use this identifier to cite or link to this item: https://doi.org/10.1038/nsmb1162
DC FieldValue
dc.titleSolution structures of the adhesion molecule DdCAD-1 reveal new insights into Ca2+-dependent cell-cell adhesion
dc.contributor.authorLin, Z.
dc.contributor.authorSriskanthadevan, S.
dc.contributor.authorHuang, H.
dc.contributor.authorSiu, C.-H.
dc.contributor.authorYang, D.
dc.date.accessioned2014-10-27T08:39:59Z
dc.date.available2014-10-27T08:39:59Z
dc.date.issued2006-11
dc.identifier.citationLin, Z., Sriskanthadevan, S., Huang, H., Siu, C.-H., Yang, D. (2006-11). Solution structures of the adhesion molecule DdCAD-1 reveal new insights into Ca2+-dependent cell-cell adhesion. Nature Structural and Molecular Biology 13 (11) : 1016-1022. ScholarBank@NUS Repository. https://doi.org/10.1038/nsmb1162
dc.identifier.issn15459993
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101696
dc.description.abstractDdCAD-1 is a novel Ca2+-dependent cell adhesion molecule that lacks a hydrophobic signal peptide and a transmembrane domain. DdCAD-1 is expressed by the social amoeba Dictyostelium discoideum at the onset of development. It is synthesized as a soluble protein and then transported to the plasma membrane by contractile vacuoles. Here we describe the novel features of the solution structures of Ca2+-free and Ca2+-bound monomeric DdCAD-1. DdCAD-1 contains two β-sandwich domains, belonging to the βγ-crystallin and immunoglobulin fold classes, respectively. Whereas the N-terminal domain has a major role in homophilic binding, the C-terminal domain tethers the protein to the cell membrane. From structural and mutational analyses, we propose a model for the Ca2+-bound DdCAD-1 dimer as a basis for understanding DdCAD-1-mediated cell-cell adhesion at the molecular level. Our results provide new insights into Ca2+-dependent mechanisms for cell-cell adhesion. © 2006 Nature Publishing Group.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/nsmb1162
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1038/nsmb1162
dc.description.sourcetitleNature Structural and Molecular Biology
dc.description.volume13
dc.description.issue11
dc.description.page1016-1022
dc.description.codenNSMBC
dc.identifier.isiut000241817700014
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

26
checked on Sep 20, 2019

WEB OF SCIENCETM
Citations

25
checked on Sep 12, 2019

Page view(s)

43
checked on Sep 7, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.