Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.

Journal article

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 VR...

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Authors: Scheeff, E; Eswaran, J; Bunkoczi, G; Knapp, S; Manning, G

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 17
• Issue: 1
• Pages: 128-138
• Publication date: 2009-01-01
• DOI: 10.1016/j.str.2008.10.018
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Binding Sites; Models, Molecular; Catalytic Domain; Adenosine Triphosphate; Protein Conformation; Phosphotransferases; Amino Acid Sequence; Molecular Sequence Data; Protein Folding