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1smh

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[[Image:1smh.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1smh| PDB=1smh | SCENE= }}
{{STRUCTURE_1smh| PDB=1smh | SCENE= }}
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'''Protein kinase A variant complex with completely ordered N-terminal helix'''
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===Protein kinase A variant complex with completely ordered N-terminal helix===
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==Overview==
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Protein kinases comprise the major enzyme family critically involved in signal transduction pathways; posttranslational modifications affect their regulation and determine signaling states. The prototype protein kinase A (PKA) possesses an N-terminal alpha-helix (Helix A) that is atypical for kinases and is thus a major distinguishing feature of PKA. Its physiological function may involve myristoylation at the N-terminus and modulation via phosphorylation at serine 10. Here we describe an unusual structure of an unmyristoylated PKA, unphosphorylated at serine 10, with a completely ordered N-terminus. Using standard conditions (e.g., PKI 5-24, ATP site ligand, MEGA-8), a novel 2-fold phosphorylated PKA variant showed the ordered N-terminus in a new crystal packing arrangement. Thus, the critical factor for structuring the N-terminus is apparently the absence of phosphorylation of Ser10. The flexibility of the N-terminus, its myristoylation, and the conformational dependence on the phosphorylation state are consistent with a functional role for myristoylation.
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The line below this paragraph, {{ABSTRACT_PUBMED_15196017}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15196017 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15196017}}
==About this Structure==
==About this Structure==
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[[Category: Ser10]]
[[Category: Ser10]]
[[Category: Signaling]]
[[Category: Signaling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:16:25 2008''

Revision as of 17:16, 28 July 2008

Template:STRUCTURE 1smh

Protein kinase A variant complex with completely ordered N-terminal helix

Template:ABSTRACT PUBMED 15196017

About this Structure

1SMH is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution., Breitenlechner C, Engh RA, Huber R, Kinzel V, Bossemeyer D, Gassel M, Biochemistry. 2004 Jun 22;43(24):7743-9. PMID:15196017

Page seeded by OCA on Mon Jul 28 20:16:25 2008

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