1sv0: Difference between revisions

Revision as of 17:50, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sv0.png

Template:STRUCTURE 1sv0

Crystal Structure Of Yan-SAM/Mae-SAM ComplexCrystal Structure Of Yan-SAM/Mae-SAM Complex

Template:ABSTRACT PUBMED 15260987

About this StructureAbout this Structure

1SV0 is a Protein complex structure of sequences 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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure Of Yan-SAM/Mae-SAM Complex'''
+===Crystal Structure Of Yan-SAM/Mae-SAM Complex===
-==Overview==
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-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.
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