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Structural characterization of NRAS isoform 5.

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.

SUBMITTER: Markowitz J

PROVIDER: S-EPMC4838646 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

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Structural characterization of NRAS isoform 5.

Markowitz Joseph J Mal Tapas K TK Yuan Chunhua C Courtney Nicholas B NB Patel Mitra M Stiff Andrew R AR Blachly James J Walker Christopher C Eisfeld Ann-Kathrin AK de la Chapelle Albert A Carson William E WE

Protein science : a publication of the Protein Society 20160324 5

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 solutio ...[more]

PMID: 26947772

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