4A3P

Structure of USP15 DUSP-UBL deletion mutant

4A3P の概要

• エントリーDOI: 10.2210/pdb4a3p/pdb
• 関連するPDBエントリー: 1W6V 4A3O
• 分子名称: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15, ACETATE ION, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25330.28

構造登録者

Elliott, P.R.,Liu, H.,Pastok, M.W.,Grossmann, G.J.,Rigden, D.J.,Clague, M.J.,Urbe, S.,Barsukov, I.L. (登録日: 2011-10-03, 公開日: 2011-11-16, 最終更新日: 2023-12-20)

主引用文献

Elliott, P.R.,Liu, H.,Pastok, M.W.,Grossmann, G.J.,Rigden, D.J.,Clague, M.J.,Urbe, S.,Barsukov, I.L.
Structural Variability of the Ubiquitin Specific Protease Dusp-Ubl Double Domains.
FEBS Lett., 585:3385-, 2011

PubMed Abstract: USP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. The DUSP domain and the UBL domain in these proteins are juxtaposed which may provide a functional unit conferring specificity. We determined the structures of the USP15 DUSP-UBL double domain unit in monomeric and dimeric states. We then conducted comparative analysis of the structural and physical properties of all three DUSP-UBL units. We identified structural features that dictate different dispositions between constituent domains, which in turn may influence respective binding properties.

PubMed: 22001210
DOI: 10.1016/J.FEBSLET.2011.09.040

実験手法

X-RAY DIFFRACTION (1.4 Å)