1P9C

NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a

1P9C の概要

• エントリーDOI: 10.2210/pdb1p9c/pdb
• 関連するPDBエントリー: 1P98 1P9D
• 分子名称: 26S proteasome non-ATPase regulatory subunit 4 (1 entity in total)
• 機能のキーワード: alpha helix, hairpin loop, ligand binding protein
• 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: 4916.34

構造登録者

Mueller, T.D.,Feigon, J. (登録日: 2003-05-10, 公開日: 2003-10-07, 最終更新日: 2024-05-22)

主引用文献

Mueller, T.D.,Feigon, J.
Structural determinants for the binding of ubiquitin-like domains to the proteasome.
Embo J., 22:4634-4645, 2003

PubMed Abstract: HHR23A, a protein implicated in nucleotide excision repair, belongs to a class of proteins containing both a ubiquitin-like (Ubl) domain and one or more ubiquitin-associated (UBA) domains, suggesting a role in the ubiquitin-proteasome pathway as well. The Ubl domain binds with high affinity to the second ubiquitin-interacting motif (UIM) of the S5a subunit of the proteasome. Here we present the solution structures of the HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2 complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The S5a UIM forms an alpha-helix with an unexpected hairpin loop that contributes to the binding interface with Ubl. The molecular determinants of the Ubl-proteasome interaction are revealed by analysis of the structures, chemical shift mapping, mutant binding studies and sequence conservation.

PubMed: 12970176
DOI: 10.1093/emboj/cdg467

実験手法

SOLUTION NMR