 |
PDBsum entry 2lz6
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
2lz6
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Distinct ubiquitin binding modes exhibited by sh3 domains: molecular determinants and functional implications.
|
|
|
Authors
|
|
J.L.Ortega roldan,
S.Casares,
M.Ringkjøbing jensen,
N.Cárdenes,
J.Bravo,
M.Blackledge,
A.I.Azuaga,
N.A.Van nuland.
|
|
|
Ref.
|
|
Plos One, 2013,
8,
e73018.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
SH3 domains constitute a new type of ubiquitin-binding domains. We previously
showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an
alternative orientation. We have determined the structure of the complex between
first CD2AP SH3 domain and ubiquitin and performed a structural and mutational
analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We
found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C
domain does not abrogate ubiquitin binding, in contrast to previous hypothesis
and our findings for the first two CD2AP SH3 domains. The similar alternative
binding mode of the SH3-C domains of these related adaptor proteins is
characterised by a higher affinity to C-terminal extended ubiquitin molecules.
We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes
a new ubiquitin-binding mode involved in a different cellular function and thus
changes the previously established mechanism of EGF-dependent CD2AP/CIN85
mono-ubiquitination.
|
|
|
|
|
|
|
