1UR6

NMR based structural model of the UbcH5B-CNOT4 complex

1UR6 の概要

• エントリーDOI: 10.2210/pdb1ur6/pdb
• 関連するPDBエントリー: 1E4U
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2, POTENTIAL TRANSCRIPTIONAL REPRESSOR NOT4HP, ZINC ION (3 entities in total)
• 機能のキーワード: ligase, ubiquitin conjugating enzyme, ubiquitin ligase, ring finger protein, ccr4-not complex, transcription regulation
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm (Probable): O95628
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23034.15

構造登録者

Dominguez, C.,Bonvin, A.M.J.J.,Winkler, G.S.,Van Schaik, F.M.A.,Timmers, H.Th.M.,Boelens, R. (登録日: 2003-10-27, 公開日: 2004-05-07, 最終更新日: 2024-05-15)

主引用文献

Dominguez, C.,Bonvin, A.M.J.J.,Winkler, G.S.,Van Schaik, F.M.A.,Timmers, H.T.M.,Boelens, R.
Structural Model of the Ubch5B/Cnot4 Complex Revealed by Combining NMR, Mutagenesis, and Docking Approaches.
Structure, 12:633-, 2004

PubMed Abstract: The protein CNOT4 possesses an N-terminal RING finger domain that acts as an E3 ubiquitin ligase and specifically interacts with UbcH5B, a ubiquitin-conjugating enzyme. The structure of the CNOT4 RING domain has been solved and the amino acids important for the binding to UbcH5B have been mapped. Here, the residues of UbcH5B important for the binding to CNOT4 RING domain were identified by NMR chemical shift perturbation experiments, and these data were used to generate structural models of the complex with the program HADDOCK. Together with the NMR data, additional biochemical data were included in a second docking, and comparisons of the resulting model with the structure of the c-Cbl/UbcH7 complex reveal some significant differences, notably at specific residues, and give structural insights into the E2/E3 specificity.

PubMed: 15062086
DOI: 10.1016/J.STR.2004.03.004

実験手法

SOLUTION NMR
THEORETICAL MODEL