Structural characterization of NRAS isoform 5 |
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| Authors: | Joseph Markowitz Tapas K. Mal Chunhua Yuan Nicholas B. Courtney Mitra Patel Andrew R. Stiff James Blachly Christopher Walker Ann‐Kathrin Eisfeld Albert de la Chapelle William E. Carson III |
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| Affiliation: | 1. Moffitt Cancer Center Department of Cutaneous Oncology, The Ohio State University, Columbus, Ohio;2. The Ohio State University Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio;3. The Ohio State University Campus Chemical Instrument Center‐NMR, The Ohio State University, Columbus, Ohio;4. The Ohio State University Wexner Medical Center Department of Surgery, The Ohio State University, Columbus, Ohio |
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| Abstract: | It was recently discovered that the NRAS isoform 5 (20 amino acids) is expressed in melanoma and results in a more aggressive cell phenotype. This novel isoform is responsible for increased phosphorylation of downstream targets such as AKT, MEK, and ERK as well as increased cellular proliferation. This structure report describes the NMR solution structure of NRAS isoform 5 to be used as a starting point to understand its biophysical interactions. The isoform is highly flexible in aqueous solution, but forms a helix‐turn‐coil structure in the presence of trifluoroethanol as determined by NMR and CD spectroscopy. |
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| Keywords: | melanoma NMR isoform NRAS |
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