Compact Packing of Lipocalin-type Prostaglandin D Synthase Induced by Binding of Lipophilic Ligands

被引:21
|
作者
Inoue, Katsuaki [2 ]
Yagi, Naoto [2 ]
Urade, Yoshihiro [3 ]
Inui, Takashi [1 ,4 ]
机构
[1] Osaka Prefecture Univ, Grad Sch Life & Environm Sci, Lab Prot Sci, Naka Ku, Osaka 5998531, Japan
[2] Japan Synchrotron Radiat Res Inst, Res & Utilizat Div, Sayo, Hyogo 6795198, Japan
[3] Osaka Biosci Inst, Dept Mol Behav Biol, Osaka 5650874, Japan
[4] Tsu City Coll, Dept Food & Nutr, Tsu, Mie 5140112, Japan
来源
JOURNAL OF BIOCHEMISTRY | 2009年 / 145卷 / 02期
关键词
SOLUTION SCATTERING; HIGH-RESOLUTION; PROTEIN FAMILY; CENTRAL CAVITY; RETINOL; BILIRUBIN; TRACE;
D O I
10.1093/jb/mvn154
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) is a multi-functioning protein belonging to the lipocalin family, acting as a PGD(2)-synthesizing enzyme and as an extracellular transporter for small lipophilic molecules. In the present study, to clarify the conformational changes of lipocalin proteins induced by binding of lipophilic ligands, such as all-trans-retinoic acid (RA), bilirubin (BR) and biliverdin (BV), we measured small-angle X-ray scattering (SAXS) of L-PGDS and that of two other lipocalins, -lactoglobulin (LG) and retinol-binding protein (RBP). L-PGDS bound all three ligands with high affinity, while LG and RBP could bind only RA. The radius of gyration was estimated to be 19.4 for L-PGDS, and 18.8 for L-PGDS/RA, 17.3 for L-PGDS/BR and 17.8 for L-PGDS/BV complexes, indicating that L-PGDS became compact after binding of these ligands. Alternatively, the radius of gyration of LG and RBP was 20.3 and 26.2 , respectively, and was almost the same before and after RA binding. Based on the SAXS data, we found that the compact packing upon binding ligands is a special feature of L-PGDS and it may be ascribed to the conformational flexibility of L-PGDS molecule itself, which underlies the high-affinity for its ligands.
引用
收藏
页码:169 / 175
页数:7
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