3eyb | pdb_00003eyb

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

spinqualitylabelsall models 3eyb, resolution 2.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3eyb is a 4 chain structure with sequence from Branchiostoma floridae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.79Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8MX78_BRAFL Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural and functional insights into the ligand-binding domain of a nonduplicated retinoid X nuclear receptor from the invertebrate chordate amphioxus.,Tocchini-Valentini GD, Rochel N, Escriva H, Germain P, Peluso-Iltis C, Paris M, Sanglier-Cianferani S, Van Dorsselaer A, Moras D, Laudet V J Biol Chem. 2009 Jan 16;284(3):1938-48. Epub 2008 Nov 4. PMID:18986992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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