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Structural Basis for the Function of DCN-1 in Protein Neddylation.
- Source :
-
Journal of Biological Chemistry . 8/24/2007, Vol. 282 Issue 34, p24490-24494. 5p. 4 Diagrams, 1 Chart. - Publication Year :
- 2007
-
Abstract
- Covalent modification by Nedd8 (neddylation) stimulates the ubiquitin-protein isopeptide ligase (E3) activities of Cullins. DCN-1, an evolutionarily conserved protein, promotes neddylation of Cullins in vivo, binds directly to Nedd8, and associates with Cdc53 in the budding yeast Saccharomyces cerevisiae. The 1.9Å resolution structure of yeast DCN-1 shows that the region encompassing residues 66-269 has a rectangular parallelepiped-like all -helical structures, consisting of an EF-hand motif N-terminal domain and a closely juxtaposed C-terminal domain with six -helices. The EF-hand motif structure is highly similar to that of the c-Cbl ubiquitin E3 ligase. We also demonstrate that DCN-1 directly binds to Rbx-1, a factor important for protein neddylation. The structural and biochemical results are consistent with the role of DCN-1 as a scaffold protein in a multisubunit neddylation E3 ligase complex. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00219258
- Volume :
- 282
- Issue :
- 34
- Database :
- Academic Search Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 31963845
- Full Text :
- https://doi.org/10.1074/jbc.C700038200