3hf6
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Crystal structure of human tryptophan hydroxylase type 1 with bound LP-521834 and FE
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Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTryptophan hydroxylase (TPH) is a key enzyme in the synthesis of serotonin. As a neurotransmitter, serotonin plays important physiological roles both peripherally and centrally. Here we describe the discovery of substituted triazines as a novel class of tryptophan hydroxylase inhibitors. This class of TPH inhibitors can selectively reduce serotonin levels in murine intestine after oral administration without affecting levels in the brain. These TPH inhibitors may provide novel treatments for gastrointestinal disorders associated with dysregulation of the serotonergic system, such as chemotherapy-induced emesis and irritable bowel syndrome. Substituted 3-(4-(1,3,5-triazin-2-yl)-phenyl)-2-aminopropanoic acids as novel tryptophan hydroxylase inhibitors.,Jin H, Cianchetta G, Devasagayaraj A, Gu K, Marinelli B, Samala L, Scott S, Stouch T, Tunoori A, Wang Y, Zang Y, Zhang C, David Kimball S, Main AJ, Ding ZM, Sun W, Yang Q, Yu XQ, Powell DR, Wilson A, Liu Q, Shi ZC Bioorg Med Chem Lett. 2009 Sep 1;19(17):5229-32. Epub 2009 Jul 8. PMID:19631532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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