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The Three-dimensional Structure of the Liver X Receptor β Reveals a Flexible Ligand-binding Pocket That Can Accommodate Fundamentally Different Ligands

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TLDR
The structures of the liver X receptor LXRβ (NR1H2) have been determined in complexes with two synthetic ligands, T0901317 and GW3965, to 2.1 and 2.4 Å, respectively, revealing a flexible ligand-binding pocket that can adjust to accommodate fundamentally different ligands.
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This article is published in Journal of Biological Chemistry.The article was published on 2003-10-03 and is currently open access. It has received 154 citations till now.

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Journal ArticleDOI

Principles for modulation of the nuclear receptor superfamily

TL;DR: This review provides a general overview of the mechanism of action of nuclear receptors and explores the various factors that are instrumental in modulating their pharmacology.
Journal ArticleDOI

Liver X receptor biology and pharmacology: new pathways, challenges and opportunities

TL;DR: The current status of the understanding of the LXR biology and pharmacology is discussed, with an emphasis on the molecular aspects of LXR signaling that constitute the potential of LXRs as drug targets.
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Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor

TL;DR: In this article, 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.
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Nuclear Receptors and Their Selective Pharmacologic Modulators

TL;DR: The development and pharmacology of a range of selective nuclear receptor modulators are reviewed, where ligands display agonist/partial agonist-binding domain of nuclear receptors function in a tissue or gene selective manner.
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Crystal structure of a zinc-finger–RNA complex reveals two modes of molecular recognition

TL;DR: The crystal structure of a three-finger complex with 61 bases of RNA, derived from the central regions of the complete nine-finger TFIIIA–5S RNA complex, reveals two modes of zinc-finger binding, both of which differ from that in common use for DNA.
References
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Journal ArticleDOI

The CCP4 suite: programs for protein crystallography

TL;DR: The CCP4 (Collaborative Computational Project, number 4) program suite is a collection of programs and associated data and subroutine libraries which can be used for macromolecular structure determination by X-ray crystallography.
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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Improved methods for building protein models in electron density maps and the location of errors in these models.

TL;DR: In this paper, the authors describe strategies and tools that help to alleviate this problem and simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.
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AMoRe: an automated package for molecular replacement

TL;DR: In this paper, a new molecular-replacement package is presented, which is an improvement on conventional methods, based on more powerful algorithms and a new conception that enables automation and rapid solution.
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Molecular basis of agonism and antagonism in the oestrogen receptor.

TL;DR: The crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17β-oestradiol, and the selective antagonist raloxifene provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties.
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