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Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region that interacts with Ras

Autor: S D, Emerson, V S, Madison, R E, Palermo, D S, Waugh, J E, Scheffler, K L, Tsao, S E, Kiefer, S P, Liu, D C, Fry

Publikováno v: Drug design and discovery. 13(3-4)

The structure of the Ras-binding domain of human c-Raf-1 (residues 55 to 132) as determined in solution by NMR spectroscopy is presented. It consists of a five-stranded beta-sheet, a twelve residue alpha-helix, and an additional one-turn helix. The f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::524791e2b8b6410fac9993dcf9e400b1
https://pubmed.ncbi.nlm.nih.gov/8874046

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Characterization of a 78-residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with Ras-GTP

Autor: J E, Scheffler, D S, Waugh, E, Bekesi, S E, Kiefer, J E, LoSardo, A, Neri, K M, Prinzo, K L, Tsao, B, Wegrzynski, S D, Emerson

Publikováno v: The Journal of biological chemistry. 269(35)

Four overlapping peptide fragments of human c-Raf-1 (residues 55-132, 55-117, 77-132, and 77-117) were expressed in Escherichia coli as carboxyl-terminal extensions of maltose binding protein (MBP). The MBP-Raf fusions were purified by affinity chrom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::54c5f0203e34fd3a0f6a5d5eab19f8d6
https://pubmed.ncbi.nlm.nih.gov/8071362

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