2GDZ

Crystal structure of 15-hydroxyprostaglandin dehydrogenase type1, complexed with NAD+

Summary for 2GDZ

• Entry DOI: 10.2210/pdb2gdz/pdb
• Descriptor: NAD+-dependent 15-hydroxyprostaglandin dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: hydroxyprostaglandin, dehydrogenase, structural genomics, short-chain dehydrogenase/reductase, inflammation, structural genomics consortium, sgc, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P15428
• Total number of polymer chains: 1
• Total formula weight: 29842.96

Authors

Pilka, E.S.,Guo, K.,Kavanagh, K.,Von Delft, F.,Arrowsmith, C.,Weigelt, J.,Edwards, A.,Sundstrom, M.,Oppermann, U.,Structural Genomics Consortium (SGC) (deposition date: 2006-03-17, release date: 2006-04-04, Last modification date: 2023-10-25)

Primary citation

Niesen, F.H.,Schultz, L.,Jadhav, A.,Bhatia, C.,Guo, K.,Maloney, D.J.,Pilka, E.S.,Wang, M.,Oppermann, U.,Heightman, T.D.,Simeonov, A.
High-Affinity Inhibitors of Human NAD-Dependent 15-Hydroxyprostaglandin Dehydrogenase: Mechanisms of Inhibition and Structure-Activity Relationships.
Plos One, 5:e13719-e13719, 2010

PubMed Abstract: 15-Hydroxyprostaglandin dehydrogenase (15-PGDH, EC 1.1.1.141) is the key enzyme for the inactivation of prostaglandins, regulating processes such as inflammation or proliferation. The anabolic pathways of prostaglandins, especially with respect to regulation of the cyclooxygenase (COX) enzymes have been studied in detail; however, little is known about downstream events including functional interaction of prostaglandin-processing and -metabolizing enzymes. High-affinity probes for 15-PGDH will, therefore, represent important tools for further studies.

PubMed: 21072165
DOI: 10.1371/journal.pone.0013719

Experimental method

X-RAY DIFFRACTION (1.65 Å)