4imo
Crystal structure of wild type human Lipocalin PGDS in complex with substrate analog U44069Crystal structure of wild type human Lipocalin PGDS in complex with substrate analog U44069
Template:ABSTRACT PUBMED 23526831
FunctionFunction
[PTGDS_HUMAN] Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system.[1] [2]
About this StructureAbout this Structure
4imo is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Lim SM, Chen D, Teo H, Roos A, Jansson AE, Nyman T, Tresaugues L, Pervushin K, Nordlund P. Structural and dynamic insights into substrate binding and catalysis of human lipocalin prostaglandin D synthase. J Lipid Res. 2013 Jun;54(6):1630-43. doi: 10.1194/jlr.M035410. Epub 2013 Mar 22. PMID:23526831 doi:10.1194/jlr.M035410
- ↑ Tokugawa Y, Kunishige I, Kubota Y, Shimoya K, Nobunaga T, Kimura T, Saji F, Murata Y, Eguchi N, Oda H, Urade Y, Hayaishi O. Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma. Biol Reprod. 1998 Feb;58(2):600-7. PMID:9475419
- ↑ Zhou Y, Shaw N, Li Y, Zhao Y, Zhang R, Liu ZJ. Structure-function analysis of human l-prostaglandin D synthase bound with fatty acid molecules. FASEB J. 2010 Dec;24(12):4668-77. doi: 10.1096/fj.10-164863. Epub 2010 Jul 28. PMID:20667974 doi:10.1096/fj.10-164863