1nhz

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[[Image:1nhz.gif|left|200px]]<br /><applet load="1nhz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nhz.gif|left|200px]]
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caption="1nhz, resolution 2.30&Aring;" />
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'''Crystal Structure of the Antagonist Form of Glucocorticoid Receptor'''<br />
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{{Structure
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|PDB= 1nhz |SIZE=350|CAPTION= <scene name='initialview01'>1nhz</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=486:11-(4-DIMETHYLAMINO-PHENYL)-17-HYDROXY-13-METHYL-17-PROP-1-YNYL-1,2,6,7,8,11,12,13,14,15,16,17-DODEC+AHYDRO-CYCLOPENTA[A]PHENANTHREN-3-ONE'>486</scene> and <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal Structure of the Antagonist Form of Glucocorticoid Receptor'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NHZ 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=486:'>486</scene> and <scene name='pdbligand=HEZ:'>HEZ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHZ OCA].
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1NHZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHZ OCA].
==Reference==
==Reference==
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The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism., Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, Calles K, Engstrom O, Harlan J, Muchmore S, Ramqvist AK, Thorell S, Ohman L, Greer J, Gustafsson JA, Carlstedt-Duke J, Carlquist M, J Biol Chem. 2003 Jun 20;278(25):22748-54. Epub 2003 Apr 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12686538 12686538]
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The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism., Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, Calles K, Engstrom O, Harlan J, Muchmore S, Ramqvist AK, Thorell S, Ohman L, Greer J, Gustafsson JA, Carlstedt-Duke J, Carlquist M, J Biol Chem. 2003 Jun 20;278(25):22748-54. Epub 2003 Apr 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12686538 12686538]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protien-ligand complex]]
[[Category: protien-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:08 2008''

Revision as of 10:57, 20 March 2008

Image:1nhz.gif


PDB ID 1nhz

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Antagonist Form of Glucocorticoid Receptor


Contents

Overview

Here we describe the three-dimensional crystal structures of human glucocorticoid receptor ligand-binding domain (GR-LBD) in complex with the antagonist RU-486 at 2.3 A resolution and with the agonist dexamethasone ligand together with a coactivator peptide at 2.8 A. The RU-486 structure was solved in several different crystal forms, two with helix 12 intact (GR1 and GR3) and one with a protease-digested C terminus (GR2). In GR1, part of helix 12 is in a position that covers the co-activator pocket, whereas in the GR3, domain swapping is seen between the crystallographically identical subunits in the GR dimer. An arm consisting of the end of helix 11 and beyond stretches out from one molecule, and helix 12 binds to the other LBD, partly blocking the coactivator pocket of that molecule. This type of GR-LBD dimer has not been described before but might be an artifact from crystallization. Furthermore, the subunits of the GR3 dimers are covalently connected via a disulfide bond between the Cys-736 residues in the two molecules. All three RU-486 GR-LBD structures show that GR has a very flexible region between the end of helix 11 and the end of helix 12.

Disease

Known diseases associated with this structure: Cortisol resistance OMIM:[138040]

About this Structure

1NHZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism., Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, Calles K, Engstrom O, Harlan J, Muchmore S, Ramqvist AK, Thorell S, Ohman L, Greer J, Gustafsson JA, Carlstedt-Duke J, Carlquist M, J Biol Chem. 2003 Jun 20;278(25):22748-54. Epub 2003 Apr 9. PMID:12686538

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