2UZG

Zf-UBP domain of VDU1

2UZG の概要

• エントリーDOI: 10.2210/pdb2uzg/pdb
• 分子名称: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 33, ZINC ION (2 entities in total)
• 機能のキーワード: ubl conjugation pathway, de-ubiquitination, alternative splicing, metal-binding, thiol protease, ubl conjugation, zinc, vdu1, zf-ubp, protease, hydrolase, zinc-finger
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm, perinuclear region . Isoform 3: Golgi apparatus : Q8TEY7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11124.56

構造登録者

Allen, M.D.,Bycroft, M. (登録日: 2007-04-27, 公開日: 2007-05-08, 最終更新日: 2024-05-15)

主引用文献

Allen, M.D.,Bycroft, M.
The Solution Structure of the Znf Ubp Domain of Usp33/Vdu1.
Protein Sci., 16:2072-, 2007

PubMed Abstract: USP33/VDU1 is a deubiquitinating enzyme that binds to the von Hippel-Lindau tumor suppressor protein. It also regulates thyroid hormone activation by deubiquitinating type 2 iodothyronine deiodinase. USP33/VDU1 contains a ZF UBP domain, a protein module found in many proteins in the ubiquitin-proteasome system. Several ZF UBP domains have been shown to bind ubiquitin, and a structure of a complex of the ZF UBP domain of isoT/USP5 and ubiquitin is available. In the present work, the solution structure of the ZF UBP domain of USP33/VDU1 has been determined by NMR spectroscopy. The structure differs from that of the USP5 domain, which contains only one of the three Zn ions present in the USP33/VDU1 structure. The USP33/VDU1 ZnF UBP domain does not bind to ubiquitin.

PubMed: 17766394
DOI: 10.1110/PS.072967807

実験手法

SOLUTION NMR