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- Publisher
- Springer Journals
- Copyright
- Copyright © 2013 by Springer Science+Business Media Dordrecht
- Subject
- Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
- ISSN
- 1874-2718
- eISSN
- 1874-270X
- DOI
- 10.1007/s12104-013-9467-5
- pmid
- 23361378
- Publisher site
- See Article on Publisher Site
Abstract
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.
Journal
Biomolecular NMR Assignments – Springer Journals
Published: Jan 30, 2013