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1how

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{{STRUCTURE_1how| PDB=1how | SCENE= }}
{{STRUCTURE_1how| PDB=1how | SCENE= }}
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'''THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST'''
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===THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST===
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==Overview==
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Sky1p is the only member of the SR protein kinase (SRPK) family in Saccharomyces cerevisiae. SRPKs are constitutively active kinases that display remarkable substrate specificity and have been implicated in RNA processing. Here we present the three-dimensional structure of a fully active truncated Sky1p. Analysis of the structure and structure-based functional studies reveal that the C-terminal tail, an unusual Glu residue located in the P+1 loop, and a unique mechanism for the positioning of helix alpha C act together to render Sky1p constitutively active. We have modeled a substrate peptide bound to Sky1p. The modeled complex combined with mutagenesis studies illustrate the molecular basis for substrate recognition by this kinase and suggest a mechanism by which SRPKs catalyze a sequential phosphorylation reaction of the consecutive RS dipeptide repeats characteristic of mammalian SRPK substrates.
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The line below this paragraph, {{ABSTRACT_PUBMED_11175909}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11175909 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11175909}}
==About this Structure==
==About this Structure==
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[[Category: Yun, C Y.]]
[[Category: Yun, C Y.]]
[[Category: Kinase]]
[[Category: Kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:04:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:28:49 2008''

Revision as of 05:28, 1 July 2008

Template:STRUCTURE 1how

THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST

Template:ABSTRACT PUBMED 11175909

About this Structure

1HOW is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The structure of Sky1p reveals a novel mechanism for constitutive activity., Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, Ghosh G, Nat Struct Biol. 2001 Feb;8(2):176-83. PMID:11175909

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