1sv0
From Proteopedia
Crystal Structure Of Yan-SAM/Mae-SAM Complex
Structural highlights
Function[POK_DROME] Negative regulator of photoreceptor development that acts antagonistically to the proneural signal mediated by RAS. It acts upstream of SINA to inhibit R7 development.[1] [2] 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 PubMedYan, 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Drome | Large Structures | Bowie, J U | Courey, A J | Gingery, M | Hunter, J B | Kim, C A | Qiao, F | Rebay, I | Sawaya, M R | Song, H | Alpha-helix | Transcription
