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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

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Publisher copy:
10.1016/j.str.2008.10.018

Authors


Scheeff, ED More by this author
Eswaran, J More by this author
Bunkoczi, G More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Manning, G More by this author
Journal:
Structure (London, England : 1993)
Volume:
17
Issue:
1
Pages:
128-138
Publication date:
2009-01-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:a9910e8c-5524-4c43-8cde-1b19f2ffabf2
Source identifiers:
41077
Local pid:
pubs:41077

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