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...
| Principais autores: | , , , , |
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| Formato: | Journal article |
| Idioma: | English |
| Publicado em: |
Cell Press
2009
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| Assuntos: |