1K2P

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.

(2001) J Biol Chem 276: 41435-41443

• PubMed: 11527964 Search on PubMed
• DOI: https://doi.org/10.1074/jbc.M104828200
• Primary Citation of Related Structures:  
  1K2P


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

Department of Structural Biology, Parker Hughes Cancer Center, St. Paul, Minnesota 55113, USA. [email protected]