- Abstract:
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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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 1.9MB)
-
- Publisher copy:
- 10.1016/j.str.2008.10.018
-
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- Publisher:
- Cell Press Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 17
- Issue:
- 1
- Pages:
- 128-38
- Publication date:
- 2009-01-01
- DOI:
- ISSN:
-
0969-2126
- URN:
-
uuid:1780d073-bb26-4687-b799-ff5ab11aef8f
- Local pid:
- SGC:19141289
- Copyright holder:
- Wellcome Trust, US Department of Health and Human Services, National Human Genome Research Institute, National Institutes of Health, and Elsevier Ltd
- Copyright date:
- 2009
- Notes:
- Copyright © 2009 Elsevier Ltd. Open access under CC BY license.
Journal article
Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site.
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