(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.
复制标题
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
复制
发表时间:
2014
影响因子:
0.9
通讯作者:
Ohkubo Tadayasu.
中科院分区:
文献类型:
--
作者:
Shimamoto Shigeru;Maruo Hiroko;Yoshida Takuya;Ohkubo Tadayasu.
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.