1lo1: Difference between revisions
New page: left|200px<br /> <applet load="1lo1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lo1" /> '''ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOM... |
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'''ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA'''<br /> | '''ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA'''<br /> | ||
==Overview== | ==Overview== | ||
While most nuclear receptors bind DNA as homo or heterodimers, the human | 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. | ||
==Disease== | |||
Known diseases associated with this structure: Deafness, autosomal recessive 35 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602167 602167]] | |||
==About this Structure== | ==About this Structure== | ||
1LO1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1LO1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dyson, H | [[Category: Dyson, H J.]] | ||
[[Category: Evans, R | [[Category: Evans, R M.]] | ||
[[Category: Gearhart, M | [[Category: Gearhart, M D.]] | ||
[[Category: Holmbeck, S | [[Category: Holmbeck, S M.A.]] | ||
[[Category: Wright, P | [[Category: Wright, P E.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: dna binding domain]] | [[Category: dna binding domain]] | ||
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[[Category: hormone nuclear receptor]] | [[Category: hormone nuclear receptor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:41 2008'' |
Revision as of 14:46, 21 February 2008
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ESTROGEN RELATED RECEPTOR 2 DNA BINDING DOMAIN IN COMPLEX WITH DNA
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Deafness, autosomal recessive 35 OMIM:[602167]
About this StructureAbout this Structure
1LO1 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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