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Considerations on the structural evidence of a ligand-binding function of ultraspiracle, an insect homolog of vertebrate RXR.

Abstract：

:This analysis considers the structural evidence of a ligand-binding function of the nuclear receptor ultraspiracle (USP). The positions and nature of residues in the ligand-binding domain of USP from six higher insects is evaluated in comparison to the function of conserved residues vertebrate receptors that have been co-crystallized with ligand. USP appears to conserve residues that in vertebrate receptors (1) form the hydrophobic ligand-binding pocket, (2) contact oxygen-containing moieties on ligands, such as hydroxyl, keto and carboxyl groups, and (3) in response to ligand-binding conformationally change to form a multi-helix hydrophobic groove for recruitment of transcriptional co-activators. These structural features are consistent with the recent report that USP can bind the epoxymethylfarnesoates (juvenile hormones) and thereupon is induced to change conformation.

journal_name

Insect Biochem Mol Biol

journal_title

Insect biochemistry and molecular biology

authors

Jones G,Jones D

doi

10.1016/s0965-1748(00)00038-2

subject

Has Abstract

pub_date

2000-08-01 00:00:00

pages

671-9

issue

8-9

eissn

0965-1748

issn

1879-0240

pii

S0965-1748(00)00038-2

journal_volume

30

pub_type

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