In:
The EMBO Journal, EMBO, Vol. 36, No. 15 ( 2017-08), p. 2251-2262
Kurzfassung:
image The structure of the Spy1/ RINGO protein in complex with cyclin‐dependent kinase 2 (Cdk2) reveals how this cancer‐associated non‐cyclin activator induces an active Cdk conformation that is insensitive to canonical regulatory signals. Spy1 adopts a similar fold as cyclin A despite low sequence homology to cyclins. Like cyclin A, Spy1 binds Cdk2 to properly organize the kinase active site. Activating T‐loop phosphorylation is dispensable for repositioning the T‐loop away from the Cdk substrate‐binding site when bound to Spy1. A cleft that in cyclins binds Cdk inhibitors such as p27 and mediates substrate specificity is absent in Spy1.
Materialart:
Online-Ressource
ISSN:
0261-4189
,
1460-2075
DOI:
10.15252/embj.201796905
Sprache:
Englisch
Verlag:
EMBO
Publikationsdatum:
2017
ZDB Id:
1467419-1
ZDB Id:
586044-1
SSG:
12