2f49: Difference between revisions

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-[[Image:2f49.jpg|left|200px]]
+{{Seed}}
+[[Image:2f49.png|left|200px]]
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 {{STRUCTURE_2f49|  PDB=2f49  |  SCENE=  }}
-'''Crystal structure of Fus3 in complex with a Ste5 peptide'''
+===Crystal structure of Fus3 in complex with a Ste5 peptide===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16424299}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16424299 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16424299}}
 ==About this Structure==
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 [[Category: Remenyi, A.]]
 [[Category: Protein-petide complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:26:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:36:06 2008''