1u3s: Difference between revisions

Revision as of 14:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1u3s.png

Template:STRUCTURE 1u3s

Crystal Structure of Estrogen Receptor beta complexed with WAY-797Crystal Structure of Estrogen Receptor beta complexed with WAY-797

Template:ABSTRACT PUBMED 15456246

About this StructureAbout this Structure

1U3S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Design and synthesis of aryl diphenolic azoles as potent and selective estrogen receptor-beta ligands., Malamas MS, Manas ES, McDevitt RE, Gunawan I, Xu ZB, Collini MD, Miller CP, Dinh T, Henderson RA, Keith JC Jr, Harris HA, J Med Chem. 2004 Oct 7;47(21):5021-40. PMID:15456246

Page seeded by OCA on Mon Jul 28 14:47:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1u3s.gif|left|200px]]
+{{Seed}}
+[[Image:1u3s.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1u3s|  PDB=1u3s  |  SCENE=  }}
-'''Crystal Structure of Estrogen Receptor beta complexed with WAY-797'''
+===Crystal Structure of Estrogen Receptor beta complexed with WAY-797===
-==Overview==
+<!--
-New diphenolic azoles as highly selective estrogen receptor-beta agonists are reported. The more potent and selective analogues of these series have comparable binding affinities for ERbeta as the natural ligand 17beta-estradiol but are &gt;100-fold selective over ERalpha. Our design strategy not only followed a traditional SAR approach but also was supported by X-ray structures of ERbeta cocrystallized with various ligands as well as molecular modeling studies. These strategies enabled us to take advantage of a single conservative residue substitution in the ligand-binding pocket, ERalpha Met(421) --&gt; ERbeta Ile(373), to optimize ERbeta selectivity. The 7-position-substituted benzoxazoles (Table 5) were the most selective ligands of both azole series, with ERB-041 (117) being &gt;200-fold selective for ERbeta. The majority of ERbeta selective agonists tested that were at least approximately 50-fold selective displayed a consistent in vivo profile: they were inactive in several models of classic estrogen action (uterotrophic, osteopenia, and vasomotor instability models) and yet were active in the HLA-B27 transgenic rat model of inflammatory bowel disease. These data suggest that ERbeta-selective agonists are devoid of classic estrogenic effects and may offer a novel therapy to treat certain inflammatory conditions.
+The line below this paragraph, {{ABSTRACT_PUBMED_15456246}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15456246 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15456246}}
 ==About this Structure==
@@ Line 41: / Line 45: @@
 [[Category: Nuclear receptor]]
 [[Category: Transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:43:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:47:57 2008''