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Journal Article

Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein

MPS-Authors
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Stier,  Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95148

Scheffzek,  Klaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://journals.iucr.org/d/issues/2004/12/02/bw5061/bw5061.pdf
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https://doi.org/10.1107/S0907444904026861
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Citation

Bonneau, F., D Angelo, I., Welti, S., Stier, G., Ylänne, J., & Scheffzek, K. (2004). Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein. Acta Crystallographica Section D-Biological Crystallography, 60(2), 2364-2367. doi:10.1107/S0907444904026861.


Cite as: https://hdl.handle.net/21.11116/0000-0001-E809-0
Abstract
Neurofibromin (MW 320 kDa) is the protein responsible for the pathogenesis of neurofibromatosis type 1 (NF1), one of the most common genetic diseases worldwide. The neurofibromin GAP-related domain (GRD, MW 38 kDa) possess a Ras-specific GTPase-activating protein property, which is at present its only clear biochemical function. This article describes the study of the bacterial production and preliminary X-ray crystallographic analysis of a neurofibromin fragment located at the C-terminal end of the GRD, which contains a region reported to be homologous to the yeast Sec14p lipid exchange protein. Of the three crystal variants obtained, a tetragonal form diffracted to a resolution of at least 2.3 A.