2f49

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{{STRUCTURE_2f49| PDB=2f49 | SCENE= }}
{{STRUCTURE_2f49| PDB=2f49 | SCENE= }}
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'''Crystal structure of Fus3 in complex with a Ste5 peptide'''
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===Crystal structure of Fus3 in complex with a Ste5 peptide===
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==Overview==
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Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.
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{{ABSTRACT_PUBMED_16424299}}
==About this Structure==
==About this Structure==
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[[Category: Remenyi, A.]]
[[Category: Remenyi, A.]]
[[Category: Protein-petide complex]]
[[Category: Protein-petide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:36:06 2008''

Revision as of 10:36, 28 July 2008

Image:2f49.png

Template:STRUCTURE 2f49

Crystal structure of Fus3 in complex with a Ste5 peptide

Template:ABSTRACT PUBMED 16424299

About this Structure

2F49 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway., Bhattacharyya RP, Remenyi A, Good MC, Bashor CJ, Falick AM, Lim WA, Science. 2006 Feb 10;311(5762):822-6. Epub 2006 Jan 19. PMID:16424299

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