| Literature DB >> 18342604 |
Jacky Chi Ki Ngo1, Kayla Giang, Sutapa Chakrabarti, Chen-Ting Ma, Nhat Huynh, Jonathan C Hagopian, Pieter C Dorrestein, Xiang-Dong Fu, Joseph A Adams, Gourisankar Ghosh.
Abstract
The 2.9 A 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 beta 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.Entities:
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Year: 2008 PMID： 18342604 PMCID： PMC2852395 DOI： 10.1016/j.molcel.2007.12.017
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970