1e3k

From Proteopedia

(Difference between revisions)

Revision as of 07:59, 13 December 2017

human Progesteron Receptor Ligand Binding Domain in complex with the ligand metribolone (R1881)

Structural highlights

1e3k is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1a28
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRGR_HUMAN] The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation.^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[15]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pierson-Mullany LK, Lange CA. Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2. Mol Cell Biol. 2004 Dec;24(24):10542-57. PMID:15572662 doi:10.1128/MCB.24.24.10542-10557.2004
↑ Narayanan R, Edwards DP, Weigel NL. Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity. Mol Cell Biol. 2005 Apr;25(8):2885-98. PMID:15798179 doi:25/8/2885
↑ Man JH, Li HY, Zhang PJ, Zhou T, He K, Pan X, Liang B, Li AL, Zhao J, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM. PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus. Nucleic Acids Res. 2006;34(19):5552-66. Epub 2006 Oct 4. PMID:17020914 doi:gkl691
↑ Zhang PJ, Zhao J, Li HY, Man JH, He K, Zhou T, Pan X, Li AL, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM. CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome. EMBO J. 2007 Apr 4;26(7):1831-42. Epub 2007 Mar 8. PMID:17347654 doi:7601602
↑ Daniel AR, Faivre EJ, Lange CA. Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells. Mol Endocrinol. 2007 Dec;21(12):2890-906. Epub 2007 Aug 23. PMID:17717077 doi:me.2007-0248
↑ Daniel AR, Qiu M, Faivre EJ, Ostrander JH, Skildum A, Lange CA. Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth. Steroids. 2007 Feb;72(2):188-201. Epub 2006 Dec 14. PMID:17173941 doi:S0039-128X(06)00225-X
↑ Faivre EJ, Daniel AR, Hillard CJ, Lange CA. Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors. Mol Endocrinol. 2008 Apr;22(4):823-37. Epub 2008 Jan 17. PMID:18202149 doi:me.2007-0437
↑ Pierson-Mullany LK, Lange CA. Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2. Mol Cell Biol. 2004 Dec;24(24):10542-57. PMID:15572662 doi:10.1128/MCB.24.24.10542-10557.2004
↑ Narayanan R, Edwards DP, Weigel NL. Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity. Mol Cell Biol. 2005 Apr;25(8):2885-98. PMID:15798179 doi:25/8/2885
↑ Man JH, Li HY, Zhang PJ, Zhou T, He K, Pan X, Liang B, Li AL, Zhao J, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM. PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus. Nucleic Acids Res. 2006;34(19):5552-66. Epub 2006 Oct 4. PMID:17020914 doi:gkl691
↑ Zhang PJ, Zhao J, Li HY, Man JH, He K, Zhou T, Pan X, Li AL, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM. CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome. EMBO J. 2007 Apr 4;26(7):1831-42. Epub 2007 Mar 8. PMID:17347654 doi:7601602
↑ Daniel AR, Faivre EJ, Lange CA. Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells. Mol Endocrinol. 2007 Dec;21(12):2890-906. Epub 2007 Aug 23. PMID:17717077 doi:me.2007-0248
↑ Daniel AR, Qiu M, Faivre EJ, Ostrander JH, Skildum A, Lange CA. Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth. Steroids. 2007 Feb;72(2):188-201. Epub 2006 Dec 14. PMID:17173941 doi:S0039-128X(06)00225-X
↑ Faivre EJ, Daniel AR, Hillard CJ, Lange CA. Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors. Mol Endocrinol. 2008 Apr;22(4):823-37. Epub 2008 Jan 17. PMID:18202149 doi:me.2007-0437
↑ 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. Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. J Biol Chem. 2000 Aug 25;275(34):26164-71. PMID:10840043 doi:http://dx.doi.org/10.1074/jbc.M004571200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e3k"

@@ Line 1: / Line 1: @@
-==HUMAN PROGESTERON RECEPTOR LIGAND BINDING DOMAIN IN COMPLEX WITH THE LIGAND METRIBOLONE (R1881)==
+==human Progesteron Receptor Ligand Binding Domain in complex with the ligand metribolone (R1881)==
 <StructureSection load='1e3k' size='340' side='right' caption='[[1e3k]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=R18:(17BETA)-17-HYDROXY-17-METHYLESTRA-4,9,11-TRIEN-3-ONE'>R18</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a28|1a28]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3k OCA], [http://pdbe.org/1e3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e3k RCSB], [http://www.ebi.ac.uk/pdbsum/1e3k PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3k OCA], [http://pdbe.org/1e3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e3k RCSB], [http://www.ebi.ac.uk/pdbsum/1e3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e3k ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e3k_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e3k_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1e3k

From Proteopedia

Revision as of 07:59, 13 December 2017

human Progesteron Receptor Ligand Binding Domain in complex with the ligand metribolone (R1881)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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