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~~'''~~Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2~~'''~~

===Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_18342604}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18342604 is the PubMed ID number.

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==About this Structure==

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[[Category: Transferase]]

[[Category: Transferase/splicing complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Apr 9 14~~:45:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:49:02 2008''

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-[[Image:3beg.jpg|left|200px]]
+{{Seed}}
+[[Image:3beg.png|left|200px]]
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 {{STRUCTURE_3beg|  PDB=3beg  |  SCENE=  }}
-'''Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2'''
+===Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18342604}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18342604 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18342604}}
 ==About this Structure==
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 [[Category: Transferase]]
 [[Category: Transferase/splicing complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr  9 14:45:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:49:02 2008''