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

Abstract:

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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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.str.2008.10.018

Authors


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

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