1r4r

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(New page: 200px<br /><applet load="1r4r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4r, resolution 3.0&Aring;" /> '''Crystallographic anal...)
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[[Image:1r4r.gif|left|200px]]<br /><applet load="1r4r" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r4r.gif|left|200px]]<br /><applet load="1r4r" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1r4r, resolution 3.0&Aring;" />
caption="1r4r, resolution 3.0&Aring;" />
'''Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA'''<br />
'''Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA'''<br />
==Overview==
==Overview==
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Two crystal structures of the glucocorticoid receptor DNA-binding domain, complexed with DNA are reported. The domain has a globular fold which, contains two Zn-nucleated substructures of distinct conformation and, function. When it binds DNA, the domain dimerizes, placing the subunits in, adjacent major grooves. In one complex, the DNA has the symmetrical, consensus target sequence; in the second, the central spacing between the, target's half-sites is larger by one base pair. This results in one, subunit interacting specifically with the consensus target half-site and, the other nonspecifically with a noncognate element. The DNA-induced dimer, fixes the separation of the subunits' recognition surfaces so that the, spacing between the half-sites becomes a critical feature of the target, sequence's identity.
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Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported. The domain has a globular fold which contains two Zn-nucleated substructures of distinct conformation and function. When it binds DNA, the domain dimerizes, placing the subunits in adjacent major grooves. In one complex, the DNA has the symmetrical consensus target sequence; in the second, the central spacing between the target's half-sites is larger by one base pair. This results in one subunit interacting specifically with the consensus target half-site and the other nonspecifically with a noncognate element. The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity.
==About this Structure==
==About this Structure==
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1R4R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1R4R OCA].
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1R4R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] 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=1R4R OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Freedman, L.P.]]
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[[Category: Freedman, L P.]]
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[[Category: Luisi, B.F.]]
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[[Category: Luisi, B F.]]
[[Category: Otwinowski, Z.]]
[[Category: Otwinowski, Z.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
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[[Category: Xu, W.X.]]
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[[Category: Xu, W X.]]
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[[Category: Yamamoto, K.R.]]
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[[Category: Yamamoto, K R.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: glucocorticoid]]
[[Category: glucocorticoid]]
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[[Category: steroid receptor]]
[[Category: steroid receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:15:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:00 2008''

Revision as of 12:47, 21 February 2008


1r4r, resolution 3.0Å

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Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA

Overview

Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported. The domain has a globular fold which contains two Zn-nucleated substructures of distinct conformation and function. When it binds DNA, the domain dimerizes, placing the subunits in adjacent major grooves. In one complex, the DNA has the symmetrical consensus target sequence; in the second, the central spacing between the target's half-sites is larger by one base pair. This results in one subunit interacting specifically with the consensus target half-site and the other nonspecifically with a noncognate element. The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity.

About this Structure

1R4R is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA., Luisi BF, Xu WX, Otwinowski Z, Freedman LP, Yamamoto KR, Sigler PB, Nature. 1991 Aug 8;352(6335):497-505. PMID:1865905

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