1J8C

Solution Structure of the Ubiquitin-like Domain of hPLIC-2

1J8C の概要

• エントリーDOI: 10.2210/pdb1j8c/pdb
• 分子名称: ubiquitin-like protein hPLIC-2 (1 entity in total)
• 機能のキーワード: ubiquitin-like domain, structural genomics
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q9UHD9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13637.36

構造登録者

Walters, K.J.,Kleijnen, M.F.,Goh, A.M.,Wagner, G.,Howley, P.M. (登録日: 2001-05-21, 公開日: 2002-03-20, 最終更新日: 2024-05-22)

主引用文献

Walters, K.J.,Kleijnen, M.F.,Goh, A.M.,Wagner, G.,Howley, P.M.
Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a.
Biochemistry, 41:1767-1777, 2002

PubMed Abstract: The 26S proteasome is essential for the proteolysis of proteins that have been covalently modified by the attachment of polyubiquitinated chains. Although the 20S core particle performs the degradation, the 19S regulatory cap complex is responsible for recognition of polyubiquitinated substrates. We have focused on how the S5a component of the 19S complex interacts with different ubiquitin-like (ubl) modules, to advance our understanding of how polyubiquitinated proteins are targeted to the proteasome. To achieve this, we have determined the solution structure of the ubl domain of hPLIC-2 and obtained a structural model of hHR23a by using NMR spectroscopy and homology modeling. We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces. We provide evidence that the S5a-binding surface on the ubl domain of hPLIC-2 is required for its interaction with the proteasome. This study provides structural insights into protein recognition by the proteasome, and illustrates how the protein surface of a commonly utilized fold has highly evolved for various biological roles.

PubMed: 11827521
DOI: 10.1021/bi011892y

実験手法

SOLUTION NMR