Abstract
The Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras.
Publication types
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Comparative Study
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Letter
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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DNA Mutational Analysis
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GTP-Binding Proteins / chemistry*
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GTP-Binding Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / metabolism
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Protein Structure, Secondary
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Proto-Oncogene Proteins / chemistry
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-raf
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Proto-Oncogene Proteins p21(ras) / chemistry*
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Proto-Oncogene Proteins p21(ras) / metabolism
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Sequence Alignment
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Ubiquitins / chemistry
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ral Guanine Nucleotide Exchange Factor
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rap GTP-Binding Proteins
Substances
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Peptide Fragments
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Proto-Oncogene Proteins
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Ubiquitins
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ral Guanine Nucleotide Exchange Factor
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Protein Serine-Threonine Kinases
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Proto-Oncogene Proteins c-raf
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GTP-Binding Proteins
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Proto-Oncogene Proteins p21(ras)
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rap GTP-Binding Proteins