1r20

<table><tr><td colspan='2'>[[1r20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloridea_virescens Chloridea virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R20 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=HWG:N-(TERT-BUTYL)-3,5-DIMETHYL-N-[(5-METHYL-2,3-DIHYDRO-1,4-BENZODIOXIN-6-YL)CARBONYL]BENZOHYDRAZIDE'>HWG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r1k|1r1k]]</div></td></tr>

[[https://www.uniprot.org/uniprot/ECR_HELVI ECR_HELVI]] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:14595375</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1r20" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Chloridea virescens]]

[[Category: Billas, I M.L]]

[[Category: Garnier, J M]]

[[Category: Iwema, T]]

[[Category: Mitschler, A]]

[[Category: Moras, D]]

[[Category: Rochel, N]]

[[Category: Structural proteomics in europe]]