Mutations in cystic fibrosis

Personal project
Project Overview
This poster was created during my graduate studies in the Biomedical Communications program at the University of Toronto. It is a novel data visualization that shows the frequencies and consequences of a subset of cystic fibrosis mutations, as well as their positions along the cystic fibrosis transmembrane conductance regulator (CFTR) protein sequence. Key amino acid residues that play an important role in CFTR protein function are also depicted in the data visualization.
Data was obtained from the CFTR2 database.
Tools
Adobe Illustrator
Circos
Tableau Public
References
  • CFTR2 database
  • Chin S, Yang D, Miles AJ, et al. Attenuation of Phosphorylation-dependent Activation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by Disease-causing Mutations at the Transmission Interface. The Journal of Biological Chemistry. 2017;292(5):1988-1999. doi:10.1074/jbc.M116.762633.
  • Das J, Aleksandrov AA, Cui L, He L, Riordan JR, Dokholyan NV. Transmembrane helical interactions in the CFTR channel pore. Jacobs D, ed. PLoS Computational Biology. 2017;13(6):e1005594. doi:10.1371/journal.pcbi.1005594.
  • Hwang T-C, Sheppard DN. Gating of the CFTR Cl− channel by ATP-driven nucleotide-binding domain dimerisation. The Journal of Physiology. 2009;587(Pt 10):2151-2161. doi:10.1113/jphysiol.2009.171595.
  • Loo TW, Bartlett MC, Clarke DM. The V510D Suppressor Mutation Stabilizes ΔF508-CFTR at the Cell Surface. Biochemistry. 2010;49(30):6352-6357. doi:10.1021/bi100807h.
  • Mense M, Vergani P, White DM, Altberg G, Nairn AC, Gadsby DC. In vivophosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer. The EMBO Journal. 2006;25(20):4728-4739. doi:10.1038/sj.emboj.7601373.
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