1t5z

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[[Image:1t5z.gif|left|200px]]<br /><applet load="1t5z" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1t5z.gif|left|200px]]
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caption="1t5z, resolution 2.3&Aring;" />
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'''Crystal Structure of the Androgen Receptor Ligand Binding Domain (LBD) with DHT and a peptide derived from its physiological coactivator ARA70'''<br />
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{{Structure
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|PDB= 1t5z |SIZE=350|CAPTION= <scene name='initialview01'>1t5z</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=DHT:DIHYDROTESTOSTERONE'>DHT</scene>
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|ACTIVITY=
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|GENE= AR, NR3C4, DHTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), NCOA4, ARA70, RFG, ELE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of the Androgen Receptor Ligand Binding Domain (LBD) with DHT and a peptide derived from its physiological coactivator ARA70'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1T5Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=DHT:'>DHT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T5Z OCA].
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1T5Z is a [[Protein complex]] structure of sequences 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=1T5Z OCA].
==Reference==
==Reference==
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The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor., Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RK, J Biol Chem. 2005 Mar 4;280(9):8060-8. Epub 2004 Nov 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15563469 15563469]
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The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor., Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RK, J Biol Chem. 2005 Mar 4;280(9):8060-8. Epub 2004 Nov 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15563469 15563469]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Webb, P.]]
[[Category: Webb, P.]]
[[Category: DHT]]
[[Category: DHT]]
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[[Category: androgen receptor ligand binding domain ara70 crystal structure coactivators]]
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[[Category: androgen receptor ligand binding domain ara70 crystal structure coactivator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:18 2008''

Revision as of 12:14, 20 March 2008


PDB ID 1t5z

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Gene: AR, NR3C4, DHTR (Homo sapiens), NCOA4, ARA70, RFG, ELE1 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Androgen Receptor Ligand Binding Domain (LBD) with DHT and a peptide derived from its physiological coactivator ARA70


Contents

Overview

Androgens drive sex differentiation, bone and muscle development, and promote growth of hormone-dependent cancers by binding the nuclear androgen receptor (AR), which recruits coactivators to responsive genes. Most nuclear receptors recruit steroid receptor coactivators (SRCs) to their ligand binding domain (LBD) using a leucine-rich motif (LXXLL). AR is believed to recruit unique coactivators to its LBD using an aromatic-rich motif (FXXLF) while recruiting SRCs to its N-terminal domain (NTD) through an alternate mechanism. Here, we report that the AR-LBD interacts with both FXXLF motifs and a subset of LXXLL motifs and that contacts with these LXXLL motifs are both necessary and sufficient for SRC-mediated AR regulation of transcription. Crystal structures of the activated AR in complex with both recruitment motifs reveal that side chains unique to the AR-LBD rearrange to bind either the bulky FXXLF motifs or the more compact LXXLL motifs and that AR utilizes subsidiary contacts with LXXLL flanking sequences to discriminate between LXXLL motifs.

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], Thyroid carcinoma, papillary OMIM:[601984], Thyroid carcinoma, papillary OMIM:[606918]

About this Structure

1T5Z is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor., Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RK, J Biol Chem. 2005 Mar 4;280(9):8060-8. Epub 2004 Nov 24. PMID:15563469

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