2f49
Crystal structure of Fus3 in complex with a Ste5 peptideCrystal structure of Fus3 in complex with a Ste5 peptide
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedScaffold 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 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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