NMR resonance assignments of mouse lipocalin-type prostaglandin D synthase/prostaglandin J2 complex

被引：0
作者：
Shigeru Shimamoto
Yuta Nakahata
Yuji Hidaka
Takuya Yoshida
Tadayasu Ohkubo
机构：
[1] Kindai University,Faculty of Science and Engineering
[2] Higashi-Osaka,Graduate School of Pharmaceutical Sciences
[3] Osaka University,undefined
来源：
Biomolecular NMR Assignments | 2022年 / 16卷
关键词：
Prostaglandin D; Prostaglandin H; Prostaglandin J; Lipocalin; Lypocalin-type prostaglandin D synthase;
D O I：
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学科分类号：
摘要：
Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) catalyzes the isomerization of PGH2 to produce PGD2, an endogenous somenogen, in the brains of various mammalians. We recently reported that various other PGs also bind to L-PGDS, suggesting that it could serve as an extracellular carrier for PGs. Although the solution and crystal structure of L-PGDS has been determined, as has the structure of L-PGDS complexed PGH2 analog, a structural analysis of L-PGDS complexed with other PGs is needed in order to understand the mechanism responsible for the PG trapping. Here, we report the nearly complete 1H, 13C, and 15N backbone and side chain resonance assignments of the L-PGDS/PGJ2 complex and the binding site for PGJ2 on L-PGDS.
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页码：225 / 229
页数：4
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