A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1

被引：95

作者：

Ngo, Jacky Chi Ki ^{[1
]}

Giang, Kayla ^{[1
]}

Chakrabarti, Sutapa ^{[1
]}

Ma, Chen-Ting ^{[2
]}

Huynh, Nhat ^{[1
]}

Hagopian, Jonathan C. ^{[2
]}

Dorrestein, Pieter C. ^{[1
,2
,3
]}

Fu, Xiang-Dong ^{[4
]}

Adams, Joseph A. ^{[2
]}

Ghosh, Gourisankar ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA

[3] Univ Calif San Diego, Skaggs Sch Pharm & Pharmaceut Sci, La Jolla, CA 92093 USA

[4] Univ Calif San Diego, Dept Mol Med, La Jolla, CA 92093 USA

来源：

MOLECULAR CELL | 2008年 / 29卷 / 05期

关键词：

D O I：

10.1016/j.molcel.2007.12.017

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：

The 2.9 angstrom crystal structure of the core SRPK1:ASF/SF2 complex reveals that the N-terminal half of the basic RS domain of ASF/SF2, which is destined to be phosphorylated, is bound to an acidic docking groove of SRPK1 distal to the active site. Phosphorylation of ASF/SF2 at a single site in the C-terminal end of the RS domain generates a primed phosphoserine that binds to a basic site in the kinase. Biochemical experiments support a directional sliding of the RS peptide through the docking groove to the active site during phosphorylation, which ends with the unfolding of a 0 strand of the RRM domain and binding of the unfolded region to the docking groove. We further suggest that the priming of the first serine facilitates directional substrate translocation and efficient phosphorylation.

引用

页码：563 / 576

页数：14

共 54 条

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