- 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
- Files:
-
-
(pdf, 1.9mb)
-
- Publisher copy:
- 10.1016/j.str.2007.01.001
-
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- 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
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