3TDK

Crystal Structure of Human UDP-Glucose Dehydrogenase

Summary for 3TDK

• Entry DOI: 10.2210/pdb3tdk/pdb
• Descriptor: UDP-glucose 6-dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, URIDINE-5'-DIPHOSPHATE-GLUCOSE, ... (4 entities in total)
• Functional Keywords: open hexamer, ugdh, upg, nad, oxidoreductase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 12
• Total formula weight: 666343.98

Authors

Rajakannan, V.,Han, C.,Robinson, R. (deposition date: 2011-08-11, release date: 2011-10-26, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)