Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia.

Bruton's tyrosine kinase is intimately involved in signal transduction pathways regulating survival, activation, proliferation, and differentiation of B lineage lymphoid cells. Mutations in the human btk gene are the cause of X-linked agammaglobulinemia, a male immune deficiency disorder characterized by a lack of mature, immunoglobulin-producing B lymphocytes. We have determined ...
the x-ray crystal structure of the Bruton's tyrosine kinase kinase domain in its unphosphorylated state to a 2.1 A resolution. A comparison with the structures of other tyrosine kinases and a possible mechanism of activation unique to Bruton's tyrosine kinase are provided.
Mesh Terms:
Agammaglobulinemia, Animals, Cloning, Molecular, Crystallography, X-Ray, Enzyme Activation, Humans, Linkage (Genetics), Mice, Models, Molecular, Mutation, Missense, Phosphorylation, Protein Conformation, Protein-Tyrosine Kinases, Tyrosine, X Chromosome
J. Biol. Chem.
Date: Nov. 02, 2001
Download Curated Data For This Publication
8687
Switch View:
  • Interactions 1