2KO3
Nedd8 solution structure
Summary for 2KO3
| Entry DOI | 10.2210/pdb2ko3/pdb |
| Descriptor | NEDD8 (1 entity in total) |
| Functional Keywords | nedd8, isopeptide bond, nucleus, ubl conjugation pathway, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q15843 |
| Total number of polymer chains | 1 |
| Total formula weight | 8573.98 |
| Authors | Choi, Y.S.,Jeon, Y.H.,Cheong, C. (deposition date: 2009-09-09, release date: 2009-11-03, Last modification date: 2024-05-29) |
| Primary citation | Choi, Y.S.,Jeon, Y.H.,Ryu, K.S.,Cheong, C. 60th residues of ubiquitin and Nedd8 are located out of E2-binding surfaces, but are important for K48 ubiquitin-linkage. Febs Lett., 583:3323-3328, 2009 Cited by PubMed Abstract: Nedd8, a ubiquitin-like modifier, is covalently attached to various proteins. Although Nedd8 has higher sequence identity (57%) with ubiquitin, its conserved K48 residue cannot form covalent linkage with ubiquitin. To decipher the reason why Nedd8 cannot be an effective ubiquitin-acceptor, we compared the non-covalent interaction between Nedd8 and ubiquitin for various E2s using cross-saturation NMR technique. However, both Nedd8 and ubiquitin displayed almost identical non-covalent E2-binding properties. The K60 of Nedd8 was not present at the E2-binding surface, but its mutation to Asn converted Nedd8 into a ubiquitin-acceptor. The N60 ubiquitin mutants also displayed a decreased ubiquitin-accepting activity. These results suggest the presence of an uncharacterized determinant for the K48 ubiquitin-linkage that is not related to non-covalent E2-bindings. PubMed: 19782077DOI: 10.1016/j.febslet.2009.09.034 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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