3beg: Difference between revisions

Revision as of 06:49, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3beg.png

Template:STRUCTURE 3beg

Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2

Template:ABSTRACT PUBMED 18342604

About this StructureAbout this Structure

3BEG is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1., Ngo JC, Giang K, Chakrabarti S, Ma CT, Huynh N, Hagopian JC, Dorrestein PC, Fu XD, Adams JA, Ghosh G, Mol Cell. 2008 Mar 14;29(5):563-76. PMID:18342604

Page seeded by OCA on Tue Jul 29 06:49:02 2008

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OCA

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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.
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 ==About this Structure==
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 [[Category: Transferase]]
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