(1)H, (13)C, and (15)N resonance assignments of mouse lipocalin-type prostaglandin D synthase/substrate analog complex.

(1)H, (13)C, and (15)N resonance assignments of mouse lipocalin-type prostaglandin D synthase/substrate analog complex.
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小鼠脂质运载蛋白型前列腺素 D 合酶/底物类似物复合物的 (1)H、(13)C 和 (15)N 共振归属。

DOI:
10.1007/s12104-013-9467-5
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发表时间:
2014
影响因子:
0.9
通讯作者:
Ohkubo Tadayasu.
Ohkubo Tadayasu.
中科院分区:
生物学4区
文献类型:
--
作者:
Shimamoto Shigeru;Maruo Hiroko;Yoshida Takuya;Ohkubo Tadayasu.

文献摘要

相似文献

脂钙素型前列腺素D合成酶(Lipocalin-type Prostaglandin D synthase, L-PGDS)是多种哺乳动物大脑中的pgd2合成酶。它属于脂钙蛋白超家族,是该家族中第一个被认为是酶的成员。虽然已经确定了L-PGDS的溶液和晶体结构,以了解催化反应的分子机制,但L-PGDS与底物配合物的结构分析仍有待进行。在这里,我们提出了L-PGDS/底物模拟物(U-46619)配合物的主链和侧链共振的几乎完整的分配。本研究为进一步了解L-PGDS的底物识别机制奠定了必要的基础。
Lipocalin-type Prostaglandin D synthase (L-PGDS) acts as the PGD2-synthesizing enzyme in the brain of various mammalian species. It belongs to the lipocalin superfamily and is the first member of this family to be recognized as an enzyme. Although the solution and crystal structure of L-PGDS has been determined to understand the molecular mechanism of catalytic reaction, the structural analysis of L-PGDS in complex with its substrate remains to be performed. Here, we present the nearly complete assignment of the backbone and side chain resonances of L-PGDS/substrate analog (U-46619) complex. This study lays the essential basis for further understanding the substrate recognition mechanism of L-PGDS.