1a6y: Difference between revisions

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New page: left|200px<br /> <applet load="1a6y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a6y, resolution 2.3Å" /> '''REVERBA ORPHAN NUCLE...
 
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[[Image:1a6y.gif|left|200px]]<br />
[[Image:1a6y.gif|left|200px]]<br /><applet load="1a6y" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1a6y" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1a6y, resolution 2.3&Aring;" />
caption="1a6y, resolution 2.3&Aring;" />
'''REVERBA ORPHAN NUCLEAR RECEPTOR/DNA COMPLEX'''<br />
'''REVERBA ORPHAN NUCLEAR RECEPTOR/DNA COMPLEX'''<br />


==Overview==
==Overview==
The nuclear hormone receptors form the largest known family of, transcription factors. The current notion of receptor DNA discrimination, based solely on one major type of hexameric half-site and a highly, conserved 66-residue core DNA-binding domain (DBD), does not adequately, describe how more than 150 nonsteroid receptors differentiate among, response elements. Here, we describe the 2.3 A crystal structure of the, DNA-binding region of the orphan receptor RevErb arranged as a tandem, homodimer on its optimal response element. The structure reveals the, presence of a second major protein-DNA interface adjacent to the classical, one involving the half-sites. A sequence comparison of orphan receptors, suggests that unique minor-groove interactions involving the receptor, hinge regions impart the necessary DNA and dimerization specificity.
The nuclear hormone receptors form the largest known family of transcription factors. The current notion of receptor DNA discrimination, based solely on one major type of hexameric half-site and a highly conserved 66-residue core DNA-binding domain (DBD), does not adequately describe how more than 150 nonsteroid receptors differentiate among response elements. Here, we describe the 2.3 A crystal structure of the DNA-binding region of the orphan receptor RevErb arranged as a tandem homodimer on its optimal response element. The structure reveals the presence of a second major protein-DNA interface adjacent to the classical one involving the half-sites. A sequence comparison of orphan receptors suggests that unique minor-groove interactions involving the receptor hinge regions impart the necessary DNA and dimerization specificity.


==About this Structure==
==About this Structure==
1A6Y 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6Y OCA].  
1A6Y 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=1A6Y OCA].  


==Reference==
==Reference==
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[[Category: transcription regulation]]
[[Category: transcription regulation]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:56:15 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:34 2008''

Revision as of 12:41, 21 February 2008

File:1a6y.gif


1a6y, resolution 2.3Å

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REVERBA ORPHAN NUCLEAR RECEPTOR/DNA COMPLEX

OverviewOverview

The nuclear hormone receptors form the largest known family of transcription factors. The current notion of receptor DNA discrimination, based solely on one major type of hexameric half-site and a highly conserved 66-residue core DNA-binding domain (DBD), does not adequately describe how more than 150 nonsteroid receptors differentiate among response elements. Here, we describe the 2.3 A crystal structure of the DNA-binding region of the orphan receptor RevErb arranged as a tandem homodimer on its optimal response element. The structure reveals the presence of a second major protein-DNA interface adjacent to the classical one involving the half-sites. A sequence comparison of orphan receptors suggests that unique minor-groove interactions involving the receptor hinge regions impart the necessary DNA and dimerization specificity.

About this StructureAbout this Structure

1A6Y is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural elements of an orphan nuclear receptor-DNA complex., Zhao Q, Khorasanizadeh S, Miyoshi Y, Lazar MA, Rastinejad F, Mol Cell. 1998 May;1(6):849-61. PMID:9660968

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