Journal article
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...
Expand abstract
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Version of record, pdf, 1.9MB)
-
- Publisher copy:
- 10.1016/j.str.2008.10.018
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Bibliographic Details
- 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
Item Description
- Language:
- English
- Subjects:
- UUID:
-
uuid:1780d073-bb26-4687-b799-ff5ab11aef8f
- Local pid:
- SGC:19141289
- Deposit date:
- 2011-08-18
Related Items
Terms of use
- Copyright holder:
- National Human Genome Research Institute. US Department of Health and Human Services. National Institutes of Health. Wellcome Trust. Elsevier Ltd
- Copyright date:
- 2009
- Notes:
- Copyright © 2009 Elsevier Ltd. Open access under CC BY license.
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record