Ontology highlight
ABSTRACT:
SUBMITTER: Scheeff ED
PROVIDER: S-EPMC2639636 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature
Scheeff Eric D ED Eswaran Jeyanthy J Bunkoczi Gabor G Knapp Stefan S Manning Gerard G
Structure (London, England : 1993) 20090101 1
About 10% of all protein kinases are predicted to be enzymatically inactive pseudokinases, but the structural details of kinase inactivation have remained unclear. We present the first structure of a pseudokinase, VRK3, and that of its closest active relative, VRK2. Profound changes to the active site region underlie the loss of catalytic activity, and VRK3 cannot bind ATP because of residue substitutions in the binding pocket. However, VRK3 still shares striking structural similarity with VRK2, ...[more]