Skip Navigation



Journal of Biochemistry Advance Access published online on November 17, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn154
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
145/2/169    most recent
mvn154v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Inoue, K.
Right arrow Articles by Inui, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Inoue, K.
Right arrow Articles by Inui, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

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

Katsuaki Inoue1, Naoto Yagi1, Yoshihiro Urade2 and Takashi Inui3,4,{dagger}

1Research & Utilization Division, Japan Synchrotron Radiation Research Institute, 1-1-1 Koto, Sayo, Hyogo 679-5198; 2Department of Molecular Behavioral Biology, Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Osaka 565-0874; 3 Laboratory of Protein Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531; 4Department of Food and Nutrition, Tsu City College, 157 Ishinden-Nakano, Tsu, Mie 514-0112, Japan

{dagger}To whom correspondence should be addressed: Prof. Takashi Inui, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531, Japan. Tel: +81-72-254-9473, Fax: +81-72-254-9474, E-mail: inuit{at}bioinfo.osakafu-u.ac.jp

Received September 8, 2008; Accepted November 3, 2008


  Abstract

Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) is a multi-functioning protein belonging to the lipocalin family, acting as a PGD2-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 2 other lipocalins, β-lactoglobulin (βLG) and retinol-binding protein (RBP). L-PGDS bound all three ligands with high affinity, while βLG and RBP could bind only RA. The radius of gyration was estimated to be 19.4 Å for L-PGDS, and 18.8 Å for L-PGDS/RA, 17.3 Å for L-PGDS/BR and 17.8 Å for L-PGDS/BV complexes, indicating that L-PGDS became compact after binding of these ligands. Alternatively, the radius of gyration of βLG and RBP was 20.3 and 26.2 Å, 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.

Key Words: broad selectivity, compact packing, conformational change, radius of gyration, SAXS


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
T. Kumasaka, K. Aritake, H. Ago, D. Irikura, T. Tsurumura, M. Yamamoto, M. Miyano, Y. Urade, and O. Hayaishi
Structural Basis of the Catalytic Mechanism Operating in Open-Closed Conformers of Lipocalin Type Prostaglandin D Synthase
J. Biol. Chem., August 14, 2009; 284(33): 22344 - 22352.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.