3EYB

Structural and functional insights into the ligand binding domain of a non-duplicated RXR from the invertebrate chordate amphioxus

3EYB の概要

• エントリーDOI: 10.2210/pdb3eyb/pdb
• 分子名称: Nuclear hormone receptor RXR (2 entities in total)
• 機能のキーワード: amphioxus, retinoid x receptor, nuclear receptor, ligand binding, dna-binding, metal-binding, nucleus, receptor, transcription, transcription regulation, zinc-finger, structural genomics, structural proteomics in europe, spine
• 由来する生物種: Branchiostoma floridae (Florida lancelet)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 98790.98

構造登録者

Tocchini-Valentini, G.D.,Rochel, N.,Moras, D.,Structural Proteomics in Europe (SPINE) (登録日: 2008-10-20, 公開日: 2008-11-04, 最終更新日: 2023-09-06)

主引用文献

Tocchini-Valentini, G.D.,Rochel, N.,Escriva, H.,Germain, P.,Peluso-Iltis, C.,Paris, M.,Sanglier-Cianferani, S.,Van Dorsselaer, A.,Moras, D.,Laudet, V.
Structural and functional insights into the ligand-binding domain of a nonduplicated retinoid X nuclear receptor from the invertebrate chordate amphioxus
J.Biol.Chem., 284:1938-1948, 2009

PubMed Abstract: Retinoid X nuclear receptors (RXRs), as well as their insect orthologue, ultraspiracle protein (USP), play an important role in the transcription regulation mediated by the nuclear receptors as the common partner of many other nuclear receptors. Phylogenetic and structural studies have shown that the several evolutionary shifts have modified the ligand binding ability of RXRs. To understand the vertebrate-specific character of RXRs, we have studied the RXR ligand-binding domain of the cephalochordate amphioxus (Branchiostoma floridae), an invertebrate chordate that predates the genome duplication that produced the three vertebrates RXRs (alpha, beta, and gamma). Here we report the crystal structure of a novel apotetramer conformation of the AmphiRXR ligand-binding domain, which shows some similarity with the structures of the arthropods RXR/USPs. AmphiRXR adopts an apo antagonist conformation with a peculiar conformation of helix H11 filling the binding pocket. In contrast to the arthropods RXR/USPs, which cannot be activated by any RXR ligands, our functional data show that AmphiRXR, like the vertebrates/mollusk RXRs, is able to bind and be activated by RXR ligands but less efficiently than vertebrate RXRs. Our data suggest that amphioxus RXR is, functionally, an intermediate between arthropods RXR/USPs and vertebrate RXRs.

PubMed: 18986992
DOI: 10.1074/jbc.M805692200

実験手法

X-RAY DIFFRACTION (2.79 Å)