Dr. David Langelaan, PhD
Department of Biochemistry & Molecular Biology, Dalhousie University
Structural biology, biophysics, protein-protein interactions, melanoma
Uncovering the signals that drive cancer
Dr. Langelaan is interested in how transcription factors, which are proteins that signal for and control cell division and development, can be involved in disease. Specifically, he is investigating the MITF transcription factor that is involved with relaying the cell signals that cause melanoma. Dr. Langelaan uses a combination of structural biology and biophysics to determine the shape and structure of MITF as it partners with other proteins in the body to carry out its function. This research will lead to new strategies to design drugs to treat melanoma.
Membership Status:Dr. David Langelaan is an Associate Member
Address:Rm-8F1, Sir Charles Tupper Building, 5850 College St., Dalhousie University, Halifax NS, B3H 4R2
Grondin, J.M., Langelaan, D.N., and Smith, S.P. (2016) Quantifying protein-carbohydrate interactions by NMR. Methods in Molecular Biology. In Press
Langelaan, D.N., Liburd, J., Yang, Y., Miller, E., Chitayat, S., Crawley, S.W., Côté, G.P. and Smith, S.P. (2016) Structure of the single-lobe myosin light chain C in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition. The Journal of Biological Chemistry. 291: 19607-17.
Ding, Y., Nash, J., Berezuk, A., Khursigara, C.M., Langelaan, D.N., Smith, S.P. and Jarrell, K. (2016) Identification of the first transcriptional activator of an archaellum operon in a Euryarchaeon. Molecular Microbiology, In Press
Read, J., Clancy, E., Sarker, M., de Antueno, R., Langelaan, D.N., Parmar, H.B., Shin, K., Rainey, J.K and Duncan R. (2015) Reovirus FAST proteins drive pore formation and syncytiogenesis using a novel helix-loop-helix fusion-inducing lipid packing sensor. PLoS Pathogens. 11(6)
Denis, C.M.*, Langelaan, D.N.*, Kirlin, A.C., Chitayat, S., Munro, K., Spencer, H.L., LeBrun, D.P., and Smith, S.P. (2014) Functional redundancy between the transcriptional activation domains of E2A is mediated by binding to the KIX domain of CBP/p300. Nucleic Acids Research. 42: 7370-82.
Langelaan, D.N., Reddy, T., Banks, A.W., Dellaire, G., Dupré, D.J. and Rainey, J.K. (2013) Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking. Biochimica et Biophysica Acta - Biomembranes. 1828: 1471-83.