¹H, ¹³C, and ¹⁵N resonance assignments of mouse lipocalin-type prostaglandin D synthase/substrate analog complex.
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.
Faculty of Science and Engineering, Kinki University, 3-4-1 Kowakae, Higashiosaka, Osaka, 577-8502, Japan, sshimamoto@life.kindai.ac.jp.
Shigeru
S
Shimamoto
Hiroko
H
Maruo
Takuya
T
Yoshida
Tadayasu
T
Ohkubo
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes; D006859:Hydrogen; D019746:Intramolecular Oxidoreductases / Q000737:chemistry*; D054834:Lipocalins / Q000737:chemistry*; D051379:Mice; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D013379:Substrate Specificity
D002247:Carbon Isotopes; D054834:Lipocalins; D050505:Mutant Proteins; D009587:Nitrogen Isotopes; D006859:Hydrogen; D019746:Intramolecular Oxidoreductases; C022466:prostaglandin R2 D-isomerase