1lat
From Proteopedia
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- | [[Image:1lat.gif|left|200px]] | + | [[Image:1lat.gif|left|200px]] |
- | + | ||
- | '''GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX''' | + | {{Structure |
+ | |PDB= 1lat |SIZE=350|CAPTION= <scene name='initialview01'>1lat</scene>, resolution 1.900Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= RAT GR AMINO ACIDS 440 TO 515 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
+ | }} | ||
+ | |||
+ | '''GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1LAT is a [ | + | 1LAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7664096 7664096] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glucocorticoid receptor]] | [[Category: glucocorticoid receptor]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:39 2008'' |
Revision as of 10:28, 20 March 2008
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, resolution 1.900Å | |||||||
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Ligands: | |||||||
Gene: | RAT GR AMINO ACIDS 440 TO 515 (Rattus norvegicus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
Page seeded by OCA on Thu Mar 20 12:28:39 2008