1r20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r20.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1r20.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r20| PDB=1r20 | SCENE= }}
{{STRUCTURE_1r20| PDB=1r20 | SCENE= }}
-
'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830'''
+
===Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830===
-
==Overview==
+
<!--
-
The ecdysteroid hormones coordinate the major stages of insect development, notably moulting and metamorphosis, by binding to the ecdysone receptor (EcR); a ligand-inducible nuclear transcription factor. To bind either ligand or DNA, EcR must form a heterodimer with ultraspiracle (USP), the homologue of retinoid-X receptor. Here we report the crystal structures of the ligand-binding domains of the moth Heliothis virescens EcR-USP heterodimer in complex with the ecdysteroid ponasterone A and with a non-steroidal, lepidopteran-specific agonist BYI06830 used in agrochemical pest control. The two structures of EcR-USP emphasize the universality of heterodimerization as a general mechanism common to both vertebrates and invertebrates. Comparison of the EcR structures in complex with steroidal and non-steroidal ligands reveals radically different and only partially overlapping ligand-binding pockets that could not be predicted by molecular modelling and docking studies. These findings offer new perspectives for the design of insect-specific, environmentally safe insecticides. The concept of a ligand-dependent binding pocket in EcR provides an insight into the moulding of nuclear receptors to their ligand, and has potential applications for human nuclear receptors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14595375}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14595375 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14595375}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:10:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:05:33 2008''

Revision as of 05:05, 28 July 2008

Image:1r20.png

Template:STRUCTURE 1r20

Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830

Template:ABSTRACT PUBMED 14595375

About this Structure

1R20 is a Protein complex structure of sequences from Heliothis virescens. Full crystallographic information is available from OCA.

Reference

Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor., Billas IM, Iwema T, Garnier JM, Mitschler A, Rochel N, Moras D, Nature. 2003 Nov 6;426(6962):91-6. Epub 2003 Nov 2. PMID:14595375

Page seeded by OCA on Mon Jul 28 08:05:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r20"
Personal tools