The Structure of the Ca\(^{2+}\)-binding, Glycosylated F-spondin Domain of F-spondin - A C2-Domain Variant in an Extracellular Matrix Protein

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The Structure of the Ca\(^{2+}\)-binding, Glycosylated F-spondin Domain of F-spondin - A C2-Domain Variant in an Extracellular Matrix Protein

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Title: The Structure of the Ca\(^{2+}\)-binding, Glycosylated F-spondin Domain of F-spondin - A C2-Domain Variant in an Extracellular Matrix Protein
Author: Tan, Kemin; Lawler, Jack William

Note: Order does not necessarily reflect citation order of authors.

Citation: Tan, 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.
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Abstract: Background: 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.
Published Version: doi://10.1186/1472-6807-11-22
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117680/pdf/
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Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:7351764
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