Abstract
The three-dimensional structure of Bruton's agammaglobulinemia tyrosine kinase (Btk) SH2 domain was modeled based on v-Src. Btk SH2 is presumably very related to the other SH2 structures consisting of two beta-sheets surrounded by two alpha-helices, with a well conserved hydrophobic core and phoshotyrosyl peptide binding site. The model was used to predict the recognition sequence of the target protein, which probably is YEXI/L. Mutations in the Btk sequence can cause the human disease X-linked agammaglobulinemia and reasons for the disease in Btk SH2 mutations were inferred from the model.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Agammaglobulinaemia Tyrosine Kinase
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Agammaglobulinemia / genetics*
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Amino Acid Sequence
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Binding Sites
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Conserved Sequence
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Crystallography, X-Ray
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DNA Transposable Elements
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Humans
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Models, Molecular
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Molecular Sequence Data
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Oncogene Protein pp60(v-src) / chemistry
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Phosphotyrosine
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Point Mutation*
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Protein Structure, Secondary*
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Protein-Tyrosine Kinases / chemistry*
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Protein-Tyrosine Kinases / genetics*
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Sequence Deletion
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Tyrosine / analogs & derivatives
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Tyrosine / metabolism
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X Chromosome*
Substances
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DNA Transposable Elements
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Phosphotyrosine
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Tyrosine
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Protein-Tyrosine Kinases
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Agammaglobulinaemia Tyrosine Kinase
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BTK protein, human
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Oncogene Protein pp60(v-src)