Structural characterization of a ribose-5-phosphate isomerase B from the pathogenic fungus Coccidioides immitis |
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Authors: | Thomas E Edwards Ariel B Abramov Eric R Smith Ruth O Baydo Jess T Leonard David J Leibly Kaitlin B Thompkins Matthew C Clifton Anna S Gardberg Bart L Staker Wesley C Van Voorhis Peter J Myler Lance J Stewart |
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Institution: | 1. Biosciences Division, Argonne National Laboratory, Midwest Center for Structural Genomics and Structural Biology Center, Argonne, IL, 60439, USA 2. Division of Experimental Pathology, Department of Pathology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA, 02215, USA
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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 1.95Å resolution. The structure reveals a Ca2+-binding C2 domain variant with an 8-stranded antiparallel β-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 Ca2+- 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. |
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