کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1934186 | 1050635 | 2008 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Crystal structure of the Bruton’s tyrosine kinase PH domain with phosphatidylinositol Crystal structure of the Bruton’s tyrosine kinase PH domain with phosphatidylinositol](/preview/png/1934186.png)
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.
Journal: Biochemical and Biophysical Research Communications - Volume 377, Issue 1, 5 December 2008, Pages 23–28