Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
Copyright policy )Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
Holding kinases at the ready About 60% of kinases only reach their active state in the presence of the molecular chaperone Hsp90 and its co-chaperone Cdc37. It is unclear how the chaperones facilitate kinase function or why only some kinases are chaperone-dependent. Verba et al. determined a 3.9 Å cryo–electron microscopy structure of Hsp90:Cdc37 in complex with the kinase Cdk4. Together, Hsp90 and Cdc37 trap the kinase in an open, partially unfolded state. Taking on this state probably has direct functional benefits. Science , this issue p. 1542
- University of California, San Francisco United States
Models, Molecular, Protein Structure, Secondary, Chaperonins, General Science & Technology, Molecular, Cyclin-Dependent Kinase 4, Cell Cycle Proteins, Biological Sciences, Protein Structure, Secondary, Models, Multiprotein Complexes, Enzyme Stability, Sf9 Cells, Animals, Humans, Biochemistry and Cell Biology, HSP90 Heat-Shock Proteins, Protein Unfolding
Models, Molecular, Protein Structure, Secondary, Chaperonins, General Science & Technology, Molecular, Cyclin-Dependent Kinase 4, Cell Cycle Proteins, Biological Sciences, Protein Structure, Secondary, Models, Multiprotein Complexes, Enzyme Stability, Sf9 Cells, Animals, Humans, Biochemistry and Cell Biology, HSP90 Heat-Shock Proteins, Protein Unfolding
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