1e3g

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(New page: 200px<br /> <applet load="1e3g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e3g, resolution 2.40&Aring;" /> '''HUMAN ANDROGEN RECE...)
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[[Image:1e3g.gif|left|200px]]<br /><applet load="1e3g" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1e3g" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1e3g, resolution 2.40&Aring;" />
caption="1e3g, resolution 2.40&Aring;" />
'''HUMAN ANDROGEN RECEPTOR LIGAND BINDING IN COMPLEX WITH THE LIGAND METRIBOLONE (R1881)'''<br />
'''HUMAN ANDROGEN RECEPTOR LIGAND BINDING IN COMPLEX WITH THE LIGAND METRIBOLONE (R1881)'''<br />
==Overview==
==Overview==
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The crystal structures of the human androgen receptor (hAR) and human, progesterone receptor ligand-binding domains in complex with the same, ligand metribolone (R1881) have been determined. Both three-dimensional, structures show the typical nuclear receptor fold. The change of two, residues in the ligand-binding pocket between the human progesterone, receptor and hAR is most likely the source for the specificity of R1881 to, the hAR. The structural implications of the 14 known mutations in the, ligand-binding pocket of the hAR ligand-binding domains associated with, either prostate cancer or the partial or complete androgen receptor, insensitivity syndrome were analyzed. The effects of most of these mutants, could be explained on the basis of the crystal structure.
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The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1E3G 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 R18 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3G OCA].
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1E3G 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=R18:'>R18</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3G OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Basler, S.]]
[[Category: Basler, S.]]
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[[Category: Carrondo, M.A.]]
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[[Category: Carrondo, M A.]]
[[Category: Coelho, R.]]
[[Category: Coelho, R.]]
[[Category: Donner, P.]]
[[Category: Donner, P.]]
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[[Category: Joschko, S.]]
[[Category: Joschko, S.]]
[[Category: Macedo, S.]]
[[Category: Macedo, S.]]
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[[Category: Matias, P.M.]]
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[[Category: Matias, P M.]]
[[Category: Otto, N.]]
[[Category: Otto, N.]]
[[Category: Peixoto, C.]]
[[Category: Peixoto, C.]]
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[[Category: ligand binding domain]]
[[Category: ligand binding domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:39:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:22 2008''

Revision as of 10:23, 21 February 2008


1e3g, resolution 2.40Å

Drag the structure with the mouse to rotate

HUMAN ANDROGEN RECEPTOR LIGAND BINDING IN COMPLEX WITH THE LIGAND METRIBOLONE (R1881)

Contents

Overview

The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.

Disease

Known diseases associated with this structure: Androgen insensitivity OMIM:[313700], Breast cancer, male, with Reifenstein syndrome OMIM:[313700], Hypospadias, perineal OMIM:[313700], Prostate cancer OMIM:[313700], Prostate cancer, susceptibility to OMIM:[313700], Spinal and bulbar muscular atrophy of Kennedy OMIM:[313700]

About this Structure

1E3G is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations., Matias PM, Donner P, Coelho R, Thomaz M, Peixoto C, Macedo S, Otto N, Joschko S, Scholz P, Wegg A, Basler S, Schafer M, Egner U, Carrondo MA, J Biol Chem. 2000 Aug 25;275(34):26164-71. PMID:10840043

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