Crystal structure of the Bruton's tyrosine kinase PH domain with phosphatidylinositol

Kazutaka Murayama, Miyuki Kato-Murayama, Chiemi Mishima, Ryogo Akasaka, Mikako Shirouzu, Yasuhisa Fukui, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


Bruton's tyrosine kinase (Btk) of the Tec family possesses a Pleckstrin homology (PH) domain, which is responsible for plasma membrane targeting. In this study, the crystal structure of the Btk PH domain in complex with dibutylyl-phosphatidylinositol-3,4,5-triphosphate was determined. The structure revealed that the Btk PH domain forms a homodimer and that each molecule binds phosphatidylinositol in the binding pocket. The side chain of Lys18 within a Btk-specific insertion in the β1-β2 loop is able to form a hydrogen bond with the diacylglycerol moiety of phosphatidylinositol. The other Btk-specific insertion in the β5-β6 loop constitutes the dimerization interface. Thus, the modes of phosphatidylinositol recognition and Btk PH domain dimerization are distinct from those of other PH domains.

Original languageEnglish
Pages (from-to)23-28
Number of pages6
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2008 Dec 5


  • Complex structure
  • Dimerization
  • Membrane targeting
  • Phosphatidylinositol
  • Pleckstrin homology domain

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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