1sv4: Difference between revisions

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New page: left|200px<br /><applet load="1sv4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sv4, resolution 2.15Å" /> '''Crystal Structure of...
 
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[[Image:1sv4.jpg|left|200px]]<br /><applet load="1sv4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1sv4.jpg|left|200px]]<br /><applet load="1sv4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1sv4, resolution 2.15&Aring;" />
caption="1sv4, resolution 2.15&Aring;" />
'''Crystal Structure of Yan-SAM'''<br />
'''Crystal Structure of Yan-SAM'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1SV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SV4 OCA].  
1SV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SV4 OCA].  


==Reference==
==Reference==
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bowie, J.U.]]
[[Category: Bowie, J U.]]
[[Category: Courey, A.J.]]
[[Category: Courey, A J.]]
[[Category: Gingery, M.]]
[[Category: Gingery, M.]]
[[Category: Hunter, J.B.]]
[[Category: Hunter, J B.]]
[[Category: Kim, C.A.]]
[[Category: Kim, C A.]]
[[Category: Qiao, F.]]
[[Category: Qiao, F.]]
[[Category: Rebay, I.]]
[[Category: Rebay, I.]]
[[Category: Sawaya, M.R.]]
[[Category: Sawaya, M R.]]
[[Category: Song, H.]]
[[Category: Song, H.]]
[[Category: 3(10)-helix]]
[[Category: 3(10)-helix]]
[[Category: alpha-helix]]
[[Category: alpha-helix]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:42:12 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:30 2008''

Revision as of 16:05, 21 February 2008

File:1sv4.jpg


1sv4, resolution 2.15Å

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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

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