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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"
caption="1sv4, resolution 2.15&Aring;" />
'''Crystal Structure of Yan-SAM'''<br />


==Overview==
==Crystal Structure of Yan-SAM==
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.
<StructureSection load='1sv4' size='340' side='right'caption='[[1sv4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sv4]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SV4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sv4 OCA], [https://pdbe.org/1sv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sv4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sv4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POK_DROME 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.<ref>PMID:1505027</ref> <ref>PMID:1495974</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1sv4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sv4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:15260987</ref>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15260987 15260987]
</div>
<div class="pdbe-citations 1sv4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bowie, J.U.]]
[[Category: Bowie JU]]
[[Category: Courey, A.J.]]
[[Category: Courey AJ]]
[[Category: Gingery, M.]]
[[Category: Gingery M]]
[[Category: Hunter, J.B.]]
[[Category: Hunter JB]]
[[Category: Kim, C.A.]]
[[Category: Kim CA]]
[[Category: Qiao, F.]]
[[Category: Qiao F]]
[[Category: Rebay, I.]]
[[Category: Rebay I]]
[[Category: Sawaya, M.R.]]
[[Category: Sawaya MR]]
[[Category: Song, H.]]
[[Category: Song H]]
[[Category: 3(10)-helix]]
[[Category: alpha-helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:42:12 2007''

Latest revision as of 09:20, 23 August 2023

Crystal Structure of Yan-SAMCrystal Structure of Yan-SAM

Structural highlights

1sv4 is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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

  1. ↑ Lai ZC, Rubin GM. Negative control of photoreceptor development in Drosophila by the product of the yan gene, an ETS domain protein. Cell. 1992 Aug 21;70(4):609-20. PMID:1505027
  2. ↑ Tei H, Nihonmatsu I, Yokokura T, Ueda R, Sano Y, Okuda T, Sato K, Hirata K, Fujita SC, Yamamoto D. pokkuri, a Drosophila gene encoding an E-26-specific (Ets) domain protein, prevents overproduction of the R7 photoreceptor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6856-60. PMID:1495974
  3. ↑ Qiao F, Song H, Kim CA, Sawaya MR, Hunter JB, Gingery M, Rebay I, Courey AJ, Bowie JU. Derepression by depolymerization; structural insights into the regulation of Yan by Mae. Cell. 2004 Jul 23;118(2):163-73. PMID:15260987 doi:10.1016/j.cell.2004.07.010

1sv4, resolution 2.15Å

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