1K2P

Crystal structure of Bruton's tyrosine kinase domain

Summary for 1K2P

• Entry DOI: 10.2210/pdb1k2p/pdb
• Descriptor: Tyrosine-protein kinase BTK (1 entity in total)
• Functional Keywords: bruton tryosine kinase, kinase domain, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q06187
• Total number of polymer chains: 2
• Total formula weight: 61496.80

Authors

Mao, C.,Zhou, M.,Uckun, F.M. (deposition date: 2001-09-28, release date: 2002-06-26, Last modification date: 2024-02-07)

Primary citation

Mao, C.,Zhou, M.,Uckun, F.M.
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.
J.Biol.Chem., 276:41435-41443, 2001

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.

PubMed: 11527964
DOI: 10.1074/jbc.M104828200

Experimental method

X-RAY DIFFRACTION (2.1 Å)