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[[Image:1lo1.gif|left|200px]]
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{{STRUCTURE_1lo1|  PDB=1lo1  |  SCENE=  }}
'''ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA'''


==ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA==
<StructureSection load='1lo1' size='340' side='right'caption='[[1lo1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lo1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LO1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1lo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo1 OCA], [https://pdbe.org/1lo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lo1 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ERR2_HUMAN ERR2_HUMAN] Defects in ESRRB are the cause of deafness autosomal recessive type 35 (DFNB35) [MIM:[https://omim.org/entry/608565 608565]. DFNB35 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:18179891</ref>
== Function ==
[https://www.uniprot.org/uniprot/ERR2_HUMAN ERR2_HUMAN] Nuclear receptor, may regulate ESR1 transcriptional activity.<ref>PMID:19755138</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/lo/1lo1_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=1lo1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
While most nuclear receptors bind DNA as homo or heterodimers, the human estrogen related receptors (hERRs) are members of a subfamily of orphan receptors that bind DNA as monomers. We have determined the solution structure of the DNA binding domain (DBD) of hERR2 bound to its cognate DNA. The structure and base interactions of the core DBD are similar to those of other nuclear receptors. However, high-affinity, sequence-specific DNA binding as a monomer necessitates formation of additional base contacts outside the core DBD. This is accomplished using a modified guanosine-binding "AT-hook" within the C-terminal extension (CTE) flanking the DBD, which makes base-specific minor groove interactions. The structure of the CTE is stabilized both by interactions with the DNA and by packing against a region of the core DBD normally reserved for dimerization. This pseudo-dimer interface provides a basis for the expansion of DNA recognition and suggests a mechanism through which dimerization may have evolved from an ancestral monomeric receptor.


==Overview==
Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition.,Gearhart MD, Holmbeck SM, Evans RM, Dyson HJ, Wright PE J Mol Biol. 2003 Apr 4;327(4):819-32. PMID:12654265<ref>PMID:12654265</ref>
While most nuclear receptors bind DNA as homo or heterodimers, the human estrogen related receptors (hERRs) are members of a subfamily of orphan receptors that bind DNA as monomers. We have determined the solution structure of the DNA binding domain (DBD) of hERR2 bound to its cognate DNA. The structure and base interactions of the core DBD are similar to those of other nuclear receptors. However, high-affinity, sequence-specific DNA binding as a monomer necessitates formation of additional base contacts outside the core DBD. This is accomplished using a modified guanosine-binding "AT-hook" within the C-terminal extension (CTE) flanking the DBD, which makes base-specific minor groove interactions. The structure of the CTE is stabilized both by interactions with the DNA and by packing against a region of the core DBD normally reserved for dimerization. This pseudo-dimer interface provides a basis for the expansion of DNA recognition and suggests a mechanism through which dimerization may have evolved from an ancestral monomeric receptor.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1LO1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO1 OCA].
</div>
<div class="pdbe-citations 1lo1" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition., Gearhart MD, Holmbeck SM, Evans RM, Dyson HJ, Wright PE, J Mol Biol. 2003 Apr 4;327(4):819-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12654265 12654265]
*[[Estrogen-related receptor 3D structures|Estrogen-related receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dyson, H J.]]
[[Category: Dyson HJ]]
[[Category: Evans, R M.]]
[[Category: Evans RM]]
[[Category: Gearhart, M D.]]
[[Category: Gearhart MD]]
[[Category: Holmbeck, S M.A.]]
[[Category: Holmbeck SMA]]
[[Category: Wright, P E.]]
[[Category: Wright PE]]
[[Category: Dna binding domain]]
[[Category: Estrogen related receptor 2]]
[[Category: Herr2]]
[[Category: Hormone nuclear receptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:06:11 2008''

Latest revision as of 11:47, 22 May 2024

ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNAESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA

Structural highlights

1lo1 is a 3 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ERR2_HUMAN Defects in ESRRB are the cause of deafness autosomal recessive type 35 (DFNB35) [MIM:608565. DFNB35 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.[1]

Function

ERR2_HUMAN Nuclear receptor, may regulate ESR1 transcriptional activity.[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

While most nuclear receptors bind DNA as homo or heterodimers, the human estrogen related receptors (hERRs) are members of a subfamily of orphan receptors that bind DNA as monomers. We have determined the solution structure of the DNA binding domain (DBD) of hERR2 bound to its cognate DNA. The structure and base interactions of the core DBD are similar to those of other nuclear receptors. However, high-affinity, sequence-specific DNA binding as a monomer necessitates formation of additional base contacts outside the core DBD. This is accomplished using a modified guanosine-binding "AT-hook" within the C-terminal extension (CTE) flanking the DBD, which makes base-specific minor groove interactions. The structure of the CTE is stabilized both by interactions with the DNA and by packing against a region of the core DBD normally reserved for dimerization. This pseudo-dimer interface provides a basis for the expansion of DNA recognition and suggests a mechanism through which dimerization may have evolved from an ancestral monomeric receptor.

Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition.,Gearhart MD, Holmbeck SM, Evans RM, Dyson HJ, Wright PE J Mol Biol. 2003 Apr 4;327(4):819-32. PMID:12654265[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Collin RW, Kalay E, Tariq M, Peters T, van der Zwaag B, Venselaar H, Oostrik J, Lee K, Ahmed ZM, Caylan R, Li Y, Spierenburg HA, Eyupoglu E, Heister A, Riazuddin S, Bahat E, Ansar M, Arslan S, Wollnik B, Brunner HG, Cremers CW, Karaguzel A, Ahmad W, Cremers FP, Vriend G, Friedman TB, Riazuddin S, Leal SM, Kremer H. Mutations of ESRRB encoding estrogen-related receptor beta cause autosomal-recessive nonsyndromic hearing impairment DFNB35. Am J Hum Genet. 2008 Jan;82(1):125-38. doi: 10.1016/j.ajhg.2007.09.008. PMID:18179891 doi:10.1016/j.ajhg.2007.09.008
  2. ↑ Bombail V, Collins F, Brown P, Saunders PT. Modulation of ER alpha transcriptional activity by the orphan nuclear receptor ERR beta and evidence for differential effects of long- and short-form splice variants. Mol Cell Endocrinol. 2010 Jan 15;314(1):53-61. doi: 10.1016/j.mce.2009.09.007., Epub 2009 Sep 13. PMID:19755138 doi:10.1016/j.mce.2009.09.007
  3. ↑ Gearhart MD, Holmbeck SM, Evans RM, Dyson HJ, Wright PE. Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition. J Mol Biol. 2003 Apr 4;327(4):819-32. PMID:12654265
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