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

被引：16

作者：

Murayama, Kazutaka ^{[1
,2
]}

Kato-Murayama, Miyuki ^{[1
]}

Mishima, Chiemi ^{[1
]}

Akasaka, Ryogo ^{[1
]}

Shirouzu, Mikako ^{[1
]}

Fakui, Yasuhisa ^{[3
]}

Yokoyama, Shigeyuki ^{[1
,4
]}

机构：

[1] RIKEN, Yokohama Inst, Syst & Struct Biol Ctr, Yokohama, Kanagawa 2300045, Japan

[2] Tohoku Univ, Grad Sch Biomed Engn, Aoba Ku, Sendai, Miyagi 9808575, Japan

[3] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan

[4] Univ Tokyo, Dept Biophys & Biochem, Grad Sch Sci, Bunkyo Ku, Tokyo 1130033, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 377卷 / 01期

关键词：

Complex structure; Pleckstrin homology domain; Phosphatidylinositol; membrane targeting; Dimerization;

D O I：

10.1016/j.bbrc.2008.09.055

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Lysl 8 within a Btk-specific insertion in the beta 1-beta 2 loop is able to form a hydrol-en bond with the diacylglycerol moiety of phosphatidylinositol. The other Btk-specific insertion in the beta 5-beta 6 loop constitutes the dimerization interface. Thus, the modes of phosphatidylinositol recognition and Btk PH domain dimerization are distinct from those of other PH domains. (C) 2008 Elsevier Inc. All rights reserved.

引用

页码：23 / 28

页数：6

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