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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
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 si...
| Autores principales: | , , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Cell Press
2009
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2639636/ https://www.ncbi.nlm.nih.gov/pubmed/19141289 http://dx.doi.org/10.1016/j.str.2008.10.018 |