1lat
From Proteopedia
(New page: 200px<br /><applet load="1lat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lat, resolution 1.900Å" /> '''GLUCOCORTICOID RECE...) |
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| - | [[Image:1lat.gif|left|200px]]<br /><applet load="1lat" size=" | + | [[Image:1lat.gif|left|200px]]<br /><applet load="1lat" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lat, resolution 1.900Å" /> | caption="1lat, resolution 1.900Å" /> | ||
'''GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX'''<br /> | '''GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Steroid receptors recognize bipartite targets composed of six base-pair | + | Steroid receptors recognize bipartite targets composed of six base-pair half-sites. There are two canonical types of half-site which differ only in their central two base pairs. The crystal structure of an estrogen receptor-like DNA-binding domain bound to the wrong type of half-site (a glucocorticoid response element) reveals an interface that resembles the specific interfaces of the glucocorticoid receptor or estrogen receptor bound to their correct response elements. The underlying stereochemical defect that weakens the non-cognate interface is a difference in the helical geometry of the incorrect DNA half-site which prevents a side-chain contact and results in a gap which is filled by at least five additional fixed water sites, imposing a potential entropic burden on the stability of the interface. |
==About this Structure== | ==About this Structure== | ||
| - | 1LAT 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:// | + | 1LAT 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=1LAT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gewirth, D | + | [[Category: Gewirth, D T.]] |
| - | [[Category: Sigler, P | + | [[Category: Sigler, P B.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: dna binding regulatory protein]] | [[Category: dna binding regulatory protein]] | ||
[[Category: glucocorticoid receptor]] | [[Category: glucocorticoid receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:10 2008'' |
Revision as of 11:43, 21 February 2008
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GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX
Overview
Steroid receptors recognize bipartite targets composed of six base-pair half-sites. There are two canonical types of half-site which differ only in their central two base pairs. The crystal structure of an estrogen receptor-like DNA-binding domain bound to the wrong type of half-site (a glucocorticoid response element) reveals an interface that resembles the specific interfaces of the glucocorticoid receptor or estrogen receptor bound to their correct response elements. The underlying stereochemical defect that weakens the non-cognate interface is a difference in the helical geometry of the incorrect DNA half-site which prevents a side-chain contact and results in a gap which is filled by at least five additional fixed water sites, imposing a potential entropic burden on the stability of the interface.
About this Structure
1LAT is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex., Gewirth DT, Sigler PB, Nat Struct Biol. 1995 May;2(5):386-94. PMID:7664096
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