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dc.contributor.authorTan, Kemin
dc.contributor.authorLawler, Jack William
dc.date.accessioned2012-01-09T20:55:09Z
dc.date.issued2011
dc.identifier.citationTan, Kemin, and Jack Lawler. 2011. The structure of the Ca\(^{2+}\)-binding, glycosylated F-spondin domain of F-spondin - A C2-domain variant in an extracellular matrix protein. BMC Structural Biology 11:22.en_US
dc.identifier.issn1472-6807en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:7351764
dc.description.abstractBackground: F-spondin is a multi-domain extracellular matrix (ECM) protein and a contact-repellent molecule that directs axon outgrowth and cell migration during development. The reelin_N domain and the F-spondin domain (FS domain) comprise a proteolytic fragment that interacts with the cell membrane and guides the projection of commissural axons to floor plate. The FS domain is found in F-spondins, mindins, M-spondin and amphiF-spondin. Results: We present the crystal structure of human F-spondin FS domain at 1.95\(\{AA}\) resolution. The structure reveals a Ca\(^{2+}\)-binding C2 domain variant with an 8-stranded antiparallel \(\beta\)-sandwich fold. Though the primary sequences of the FS domains of F-spondin and mindin are less than 36% identical, their overall structures are very similar. The unique feature of F-spondin FS domain is the presence of three disulfide bonds associated with the N- and C-termini of the domain and a highly conserved N-linked glycosylation site. The integrin-binding motif found in mindin is not conserved in the F-spondin FS domain. Conclusion: The structure of the F-spondin FS domain completes the structural studies of the multiple-domain ECM molecule. The homology of its core structure to a common Ca\(^{2+}\)- and lipid-binding C2 domain suggests that the F-spondin FS domain may be responsible for part of the membrane targeting of F-spondin in its regulation of axon development. The structural properties of the FS domain revealed in this study pave the way for further exploration into the functions of F-spondin.en_US
dc.language.isoen_USen_US
dc.publisherBioMed Centralen_US
dc.relation.isversionofdoi://10.1186/1472-6807-11-22en_US
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117680/pdf/en_US
dash.licenseLAA
dc.titleThe Structure of the Ca\(^{2+}\)-binding, Glycosylated F-spondin Domain of F-spondin - A C2-Domain Variant in an Extracellular Matrix Proteinen_US
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden_US
dc.relation.journalBMC Structural Biologyen_US
dash.depositing.authorLawler, Jack William
dc.date.available2012-01-09T20:55:09Z
dash.affiliation.otherHMS^Pathologyen_US
dc.identifier.doi10.1186/1472-6807-11-22*
dash.contributor.affiliatedLawler, Jack


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