1UR6

NMR based structural model of the UbcH5B-CNOT4 complex

Summary for 1UR6

• Entry DOI: 10.2210/pdb1ur6/pdb
• Related: 1E4U
• Descriptor: UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2, POTENTIAL TRANSCRIPTIONAL REPRESSOR NOT4HP, ZINC ION (3 entities in total)
• Functional Keywords: ligase, ubiquitin conjugating enzyme, ubiquitin ligase, ring finger protein, ccr4-not complex, transcription regulation
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm (Probable): O95628
• Total number of polymer chains: 2
• Total formula weight: 23034.15

Authors

Dominguez, C.,Bonvin, A.M.J.J.,Winkler, G.S.,Van Schaik, F.M.A.,Timmers, H.Th.M.,Boelens, R. (deposition date: 2003-10-27, release date: 2004-05-07, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR
THEORETICAL MODEL