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1ur6
From Proteopedia
| 1ur6, 5 NMR models () | |||||||||
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| Ligands: | |||||||||
| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 | ||||||||
| Domains: | UBCc, MOT2 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
NMR BASED STRUCTURAL MODEL OF THE UBCH5B-CNOT4 COMPLEX
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1UR6 is a 2 chains structure of sequences from Homo sapiens. Full experimental information is available from OCA.
Reference
- Dominguez C, Bonvin AM, Winkler GS, van Schaik FM, Timmers HT, Boelens R. Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches. Structure. 2004 Apr;12(4):633-44. PMID:15062086 doi:10.1016/j.str.2004.03.004
Page seeded by OCA on Tue Feb 17 12:46:03 2009
