1sv4: Difference between revisions
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'''Crystal Structure of Yan-SAM''' | '''Crystal Structure of Yan-SAM''' | ||
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[[Category: Sawaya, M R.]] | [[Category: Sawaya, M R.]] | ||
[[Category: Song, H.]] | [[Category: Song, H.]] | ||
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Revision as of 09:10, 3 May 2008
Crystal Structure of Yan-SAM
OverviewOverview
Yan, an ETS family transcriptional repressor, is regulated by receptor tyrosine kinase signaling via the Ras/MAPK pathway. Phosphorylation and downregulation of Yan is facilitated by a protein called Mae. Yan and Mae interact through their SAM domains. We find that repression by Yan requires the formation of a higher order structure mediated by Yan-SAM polymerization. Moreover, a crystal structure of the Yan-SAM/Mae-SAM complex shows that Mae-SAM specifically recognizes a surface on Yan-SAM that is also required for Yan-SAM polymerization. Mae-SAM binds to Yan-SAM with approximately 1000-fold higher affinity than Yan-SAM binds to itself and can effectively depolymerize Yan-SAM. Mutations on Mae that specifically disrupt its SAM domain-dependent interactions with Yan disable the derepression function of Mae in vivo. Depolymerization of Yan by Mae represents a novel mechanism of transcriptional control that sensitizes Yan for regulation by receptor tyrosine kinases.
About this StructureAbout this Structure
1SV4 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Derepression by depolymerization; structural insights into the regulation of Yan by Mae., Qiao F, Song H, Kim CA, Sawaya MR, Hunter JB, Gingery M, Rebay I, Courey AJ, Bowie JU, Cell. 2004 Jul 23;118(2):163-73. PMID:15260987 Page seeded by OCA on Sat May 3 09:10:12 2008