A Sliding Docking Interaction Is Essential for Sequential and Processive Phosphorylation of an SR Protein by SRPK1

The 2.9 Å 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-term...

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Hlavní autoři: Ngo, Jacky Chi Ki, Giang, Kayla, Chakrabarti, Sutapa, Ma, Chen-Ting, Huynh, Nhat, Hagopian, Jonathan C., Dorrestein, Pieter C., Fu, Xiang-Dong, Adams, Joseph A., Ghosh, Gourisankar
Médium: Artigo
Jazyk:Inglês
Vydáno: 2008
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Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2852395/
https://ncbi.nlm.nih.gov/pubmed/18342604
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2007.12.017
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