 |
PDBsum entry 2ko3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
2ko3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
60th residues of ubiquitin and nedd8 are located out of e2-Binding surfaces, But are important for k48 ubiquitin-Linkage.
|
|
|
Authors
|
|
Y.S.Choi,
Y.H.Jeon,
K.S.Ryu,
C.Cheong.
|
|
|
Ref.
|
|
Febs Lett, 2009,
583,
3323-3328.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
