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Article

Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase.

The Journal of biological chemistry - 14 Aug 2009

Kumasaka Takashi, Aritake Kosuke, Ago Hideo, Irikura Daisuke, Tsurumura Toshiharu, Yamamoto Masaki, Miyano Masashi, Urade Yoshihiro, Hayaishi Osamu

Abstract excerpt

Lipocalin type prostaglandin D synthase (L-PGDS) is a multifunctional protein acting as a somnogen (PGD2)-producing enzyme, an extracellular transporter of various lipophilic ligands, and an amyloid-beta chaperone in human cerebrospinal fluid. In this study, we determined the crystal structures of two different conformers of mouse L-PGDS, one with an open cavity of the beta-barrel and the other with a closed...

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Identifiers

PMID: 19546224
DOI: 10.1074/jbc.M109.018341
PMCID: PMC2755957

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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