Crystal structures of the ligand-binding domain of human peroxisome proliferator-activated receptor δ in complexes with phenylpropanoic acid derivatives and a pyridine carboxylic acid derivative.

Takuji Oyama, Kazuki Takiguchi, Hiroyuki Miyachi

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Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed, 1 citations in OpenAlex.

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5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Takuji OyamaDepartment of Biotechnology, Faculty of Life and Environmental Sciences, University of Yamanashi, Japan.ORCID 0000-0002-3411-7608

Kazuki TakiguchiDepartment of Biotechnology, Faculty of Life and Environmental Sciences, University of Yamanashi, Japan.

Hiroyuki MiyachiLead Exploration Unit, Drug Discovery Initiative, The University of Tokyo, Japan.

University of Yamanashi · JPThe University of Tokyo · JP

Funding

Japan Science and Technology Agency, Adaptable and Seamless Technology Transfer Program through Target-Driven R and D JPMJTM20NMOsaka University CR-20-02

6 · The paper itself

Abstract

Peroxisome proliferator-activated receptor δ (PPARδ) is a member of the nuclear receptor family and regulates glucose and lipid homeostasis in a ligand-dependent manner. Numerous phenylpropanoic acid derivatives targeting three PPAR subtypes (PPARα, PPARγ and PPARδ) have been developed towards the treatment of serious diseases such as lipid-metabolism disorders. In spite of the increasing attraction of PPARδ as a pharmaceutical target, only a limited number of protein-ligand complex structures are available. Here, four crystal structures of the ligand-binding domain of PPARδ in complexes with phenylpropanoic acid derivatives and a pyridine carboxylic acid derivative are described, including an updated, higher resolution version of a previous studied structure and three novel structures. These structures showed that the ligands were bound in the ligand-binding pocket of the receptor in a similar manner but with minor variations. The results could provide variable structural information for the further design and development of ligands targeting PPARδ.

Indexed as

Binding SitesCarboxylic AcidsCrystallography, X-RayHumansLigandsModels, MolecularPPAR deltaProtein ConformationPyridinesCarboxylic AcidsLigandsPPAR deltapyridinePyridinesligand-binding domainnuclear receptorsperoxisome proliferator-activated receptor δPPARδ

Identifiers

PMID35102897

DOI10.1107/S2053230X22000449

PMCPMC8805212

OpenAlexW4210721304

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