- Abstract:
-
p21-activated kinases have been classified into two groups based on their domain architecture. Group II PAKs (PAK4-6) regulate a wide variety of cellular functions, and PAK deregulation has been linked to tumor development. Structural comparison of five high-resolution structures comprising all active, monophosphorylated group II catalytic domains revealed a surprising degree of domain plasticity, including a number of catalytically productive and nonproductive conformers. Rearrangements of h...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Publisher:
- Cell Press Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 15
- Issue:
- 2
- Pages:
- 201-213
- Publication date:
- 2007
- DOI:
- ISSN:
-
0969-2126
- URN:
-
uuid:2dbb46ee-6e05-4d4e-b23b-84b31efe7a0a
- Local pid:
- SGC:17292838
- Copyright holder:
- US Department of Health and Human Services, National Institutes of Health, National Cancer Institute, and Elsevier Ltd
- Copyright date:
- 2007
- Notes:
- Copyright © 2007 Elsevier Ltd. Open access under CC BY license.
Journal article
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs
Actions
Authors
Bibliographic Details
Item Description
Terms of use
Metrics
Altmetrics
Dimensions
If you are the owner of this record, you can report an update to it here: Report update to this record