2bj4: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bj4]] is a 4 chain structure with 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=2BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BJ4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bj4]] is a 4 chain structure with 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=2BJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BJ4 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHT:4-HYDROXYTAMOXIFEN'>OHT</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHT:4-HYDROXYTAMOXIFEN'>OHT</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a52|1a52]], [[1akf|1akf]], [[1ere|1ere]], [[1err|1err]], [[1g50|1g50]], [[1gwq|1gwq]], [[1gwr|1gwr]], [[1hcp|1hcp]], [[1hcq|1hcq]], [[1l2i|1l2i]], [[1pcg|1pcg]], [[1qkt|1qkt]], [[1qku|1qku]], [[1r5k|1r5k]], [[1sj0|1sj0]], [[1uom|1uom]], [[1xp1|1xp1]], [[1xp6|1xp6]], [[1xp9|1xp9]], [[1xpc|1xpc]], [[3erd|3erd]], [[3ert|3ert]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a52|1a52]], [[1akf|1akf]], [[1ere|1ere]], [[1err|1err]], [[1g50|1g50]], [[1gwq|1gwq]], [[1gwr|1gwr]], [[1hcp|1hcp]], [[1hcq|1hcq]], [[1l2i|1l2i]], [[1pcg|1pcg]], [[1qkt|1qkt]], [[1qku|1qku]], [[1r5k|1r5k]], [[1sj0|1sj0]], [[1uom|1uom]], [[1xp1|1xp1]], [[1xp6|1xp6]], [[1xp9|1xp9]], [[1xpc|1xpc]], [[3erd|3erd]], [[3ert|3ert]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/2bj4 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=2bj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bj4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bj4 RCSB], [http://www.ebi.ac.uk/pdbsum/2bj4 PDBsum]</span></td></tr>
<table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Gustafsson, J A.]]
[[Category: Gustafsson, J A]]
[[Category: Heldring, N.]]
[[Category: Heldring, N]]
[[Category: Hubbard, R E.]]
[[Category: Hubbard, R E]]
[[Category: Kong, E.]]
[[Category: Kong, E]]
[[Category: Pike, A C.W.]]
[[Category: Pike, A C.W]]
[[Category: Treuter, E.]]
[[Category: Treuter, E]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
[[Category: Nuclear protein steroid-binding]]
[[Category: Nuclear protein steroid-binding]]

Revision as of 13:20, 8 January 2015

ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED PEPTIDE ANTAGONISTESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED PEPTIDE ANTAGONIST

Structural highlights

2bj4 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, RCSB, PDBsum

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

Recent studies have identified a series of estrogen receptor (ER)-interacting peptides that recognize sites that are distinct from the classic coregulator recruitment (AF2) region. Here, we report the structural and functional characterization of an ERalpha-specific peptide that binds to the liganded receptor in an AF2-independent manner. The 2-A crystal structure of the ER/peptide complex reveals a binding site that is centered on a shallow depression on the beta-hairpin face of the ligand-binding domain. The peptide binds in an unusual extended conformation and makes multiple contacts with the ligand-binding domain. The location and architecture of the binding site provides an insight into the peptide's ER subtype specificity and ligand interaction preferences. In vivo, an engineered coactivator containing the peptide motif is able to strongly enhance the transcriptional activity of liganded ERalpha, particularly in the presence of 4-hydroxytamoxifen. Furthermore, disruption of this binding surface alters ER's response to the coregulator TIF2. Together, these results indicate that this previously unknown interaction site represents a bona fide control surface involved in regulating receptor activity.

Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor.,Kong EH, Heldring N, Gustafsson JA, Treuter E, Hubbard RE, Pike AC Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3593-8. Epub 2005 Feb 23. PMID:15728727[1]

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

See Also

References

  1. Kong EH, Heldring N, Gustafsson JA, Treuter E, Hubbard RE, Pike AC. Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor. Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3593-8. Epub 2005 Feb 23. PMID:15728727

2bj4, resolution 2.00Å

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OCA