1ur6

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NMR BASED STRUCTURAL MODEL OF THE UBCH5B-CNOT4 COMPLEX

Overview

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.

About this Structure

1UR6 is a Protein complex structure of sequences from Homo sapiens with ZN as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.

Reference

Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches., Dominguez C, Bonvin AM, Winkler GS, van Schaik FM, Timmers HT, Boelens R, Structure. 2004 Apr;12(4):633-44. PMID:15062086

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