3TDK

Crystal Structure of Human UDP-Glucose Dehydrogenase

3TDK の概要

• エントリーDOI: 10.2210/pdb3tdk/pdb
• 分子名称: UDP-glucose 6-dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, URIDINE-5'-DIPHOSPHATE-GLUCOSE, ... (4 entities in total)
• 機能のキーワード: open hexamer, ugdh, upg, nad, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 666343.98

構造登録者

Rajakannan, V.,Han, C.,Robinson, R. (登録日: 2011-08-11, 公開日: 2011-10-26, 最終更新日: 2024-03-20)

主引用文献

Rajakannan, V.,Lee, H.S.,Chong, S.H.,Ryu, H.B.,Bae, J.Y.,Whang, E.Y.,Huh, J.W.,Cho, S.W.,Kang, L.W.,Choe, H.,Robinson, R.C.
Structural Basis of Cooperativity in Human UDP-Glucose Dehydrogenase.
Plos One, 6:e25226-e25226, 2011

PubMed Abstract: UDP-glucose dehydrogenase (UGDH) is the sole enzyme that catalyzes the conversion of UDP-glucose to UDP-glucuronic acid. The product is used in xenobiotic glucuronidation in hepatocytes and in the production of proteoglycans that are involved in promoting normal cellular growth and migration. Overproduction of proteoglycans has been implicated in the progression of certain epithelial cancers, while inhibition of UGDH diminished tumor angiogenesis in vivo. A better understanding of the conformational changes occurring during the UGDH reaction cycle will pave the way for inhibitor design and potential cancer therapeutics.

PubMed: 21984906
DOI: 10.1371/journal.pone.0025226

実験手法

X-RAY DIFFRACTION (2.8 Å)